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2. SARS-CoV-2 accessory proteins ORF7a and ORF3a use distinct mechanisms to down-regulate MHC-I surface expression

Author

Najla Arshad, Maudry Laurent-Rolle, Wesam S Ahmed, Jack Chun-Chieh Hsu, Susan M Mitchell, Joanna Pawlak, Debrup Sengupta, Kabir H Biswas, and Peter Cresswell

Subjects
Antigen Presentation, Multidisciplinary, HLA Antigens, SARS-CoV-2, Histocompatibility Antigens Class I, Humans, COVID-19, Viral Regulatory and Accessory Proteins, Peptides
Abstract

Major histocompatibility complex class I (MHC-I) molecules, which are dimers of a glycosylated polymorphic transmembrane heavy chain and the small protein β2-microglobulin (β2m), bind peptides in the endoplasmic reticulum that are generated by the cytosolic turnover of cellular proteins. In virus-infected cells these peptides may include those derived from viral proteins. Peptide-MHC-I complexes then traffic through the secretory pathway and are displayed at the cell surface where those containing viral peptides can be detected by CD8+ T lymphocytes that kill infected cells. Many viruses enhance their in vivo survival by encoding genes that downregulate MHC-I expression to avoid CD8+ T cell recognition. Here we report that two accessory proteins encoded by SARS-CoV-2, the causative agent of the ongoing COVID-19 pandemic, downregulate MHC-I expression using distinct mechanisms. One, ORF3a, a viroporin, reduces global trafficking of proteins, including MHC-I, through the secretory pathway. The second, ORF7a, interacts specifically with the MHC-I heavy chain, acting as a molecular mimic of β2m to inhibit its association. This slows the exit of properly assembled MHC-I molecules from the endoplasmic reticulum. We demonstrate that ORF7a reduces antigen presentation by the human MHC-I allele HLA-A*02:01. Thus, both ORF3a and ORF7a act post-translationally in the secretory pathway to lower surface MHC-I expression, with ORF7a exhibiting a novel and specific mechanism that allows immune evasion by SARS-CoV-2.Significance StatementViruses may down-regulate MHC class I expression on infected cells to avoid elimination by cytotoxic T cells. We report that the accessory proteins ORF7a and ORF3a of SARS-CoV-2 mediate this function and delineate the two distinct mechanisms involved. While ORF3a inhibits global protein trafficking to the cell surface, ORF7a acts specifically on MHC-I by competing with β2m for binding to the MHC-I heavy chain. This is the first account of molecular mimicry of β2m as a viral mechanism of MHC-I down-regulation to facilitate immune evasion.

Published
2022
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4. Impact of Calreticulin and Its Mutants on Endoplasmic Reticulum Function in Health and Disease

Author

Najla, Arshad and Peter, Cresswell

Subjects
Myeloproliferative Disorders, Genes, Regulator, Mutation, Humans, Calreticulin, Endoplasmic Reticulum
Abstract

The endoplasmic reticulum (ER) performs key cellular functions including protein synthesis, lipid metabolism and signaling. While these functions are spatially isolated in structurally distinct regions of the ER, there is cross-talk between the pathways. One vital player that is involved in ER function is the ER-resident protein calreticulin (CALR). It is a calcium ion-dependent lectin chaperone that primarily assists in glycoprotein synthesis in the ER as part of the protein quality control machinery. CALR also buffers calcium ion release and mediates other glycan-independent protein interactions. Mutations in CALR have been reported in a subset of chronic blood tumors called myeloproliferative neoplasms. The mutations consist of insertions or deletions in the CALR gene that all cause a + 1 bp shift in the reading frame and lead to a dramatic alteration of the amino acid sequence of the C-terminal domain of CALR. This alters CALR function and affects cell homeostasis. This chapter will discuss how CALR and mutant CALR affect ER health and disease.

Published
2021

5. Abstract 1379: Discovery of tumor-associated, immunogenic peptides presented in a patient-derived, mutant calreticulin-driven myeloproliferative neoplasm cell line

Author

Najla Arshad, Nathalie Vigneron, Cansu Cimen Bozkus, Vincent Stroobant, Stefan Naulaerts, Nina Bhardwaj, Benoît Van den Eynde, and Peter Cresswell

Subjects
Cancer Research, Oncology
Abstract

Background: Myeloproliferative neoplasms (MPNs) are a type of chronic blood cancers. A subset are driven by frameshift mutations in the calreticulin gene (CALR). The CALR protein is a lectin chaperone and primarily assists in glycoprotein folding in the endoplasmic reticulum. It is also part of the peptide loading complex, a set of proteins involved in antigen processing and peptide presentation by major histocompatibility complex class I (MHC-I) molecules. All MPN-associated frameshift mutations in CALR lead to a similar change in its C-terminal, altering its protein-protein interactions. Examples include impaired chaperone activity of mutant CALR that impacts protein homeostasis and compromised activity of the MHC-I peptide loading complex. We hypothesized that these impaired functions will alter the repertoire of peptides presented by MHC-I in mutant CALR expressing cells, which we characterized in a patient-derived, mutant-CALR-driven myeloid tumor cell line, Marimo. Methods: We carried out an immunopeptidome analysis on Marimo cell line derivates expressing either wildtype or mutant CALR to identify potential MPN-associated peptides presented by MHC-I, and validated their immunogenicity in human samples. MHC-I-peptide complexes were immunoprecipitated from these Marimo cell line derivates, followed by peptide elution and analysis by mass spectrometry. A subset of peptides that were found in the mass spectrometry analysis of mutant CALR cells but not wildtype CALR cells were tested for their immunogenicity by assaying the in vitro T cell responses they evoked. Naïve T cells from healthy donors, carrying at least one MHC-I allele that matched the Marimo cells, were primed and expanded with the selected peptides and peptide-specific T cell responses were measured by intracellular staining detecting effector cytokines IFN-γ and TNF-α. Results: 1. The expression of mutant CALR disrupts the function of the peptide loading complex, leading to reduced recruitment of MHC-I and reducing its cell surface expression by almost 40% compared to cells expressing wildtype CALR. 2. Peptide repertoire of MHC-I is significantly altered by the expression of mutant CALR. Immunopeptidomics revealed a qualitative and quantitative difference in peptides presented by cells expressing wildtype CALR vs mutant CALR 3. The immunogenicity of a curated list of 24 peptides was tested in healthy donors, and at least 6 peptides activated T cell responses. Similar testing in MPN patients is planned. Conclusions: This is the first study to investigate the impact of mutant CALR on the repertoire of peptides presented by MHC-I in myeloid cells. We discovered tumor-associated, immunogenic peptides that may serve as potential targets of immunotherapy allowing the specific elimination of mutant CALR-expressing cells, which has been a challenge in the treatment of MPNs. Citation Format: Najla Arshad, Nathalie Vigneron, Cansu Cimen Bozkus, Vincent Stroobant, Stefan Naulaerts, Nina Bhardwaj, Benoît Van den Eynde, Peter Cresswell. Discovery of tumor-associated, immunogenic peptides presented in a patient-derived, mutant calreticulin-driven myeloproliferative neoplasm cell line [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2022; 2022 Apr 8-13. Philadelphia (PA): AACR; Cancer Res 2022;82(12_Suppl):Abstract nr 1379.

Published
2022
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6. Impact of Calreticulin and Its Mutants on Endoplasmic Reticulum Function in Health and Disease

Author

Najla Arshad and Peter Cresswell

Subjects
0301 basic medicine, biology, Endoplasmic reticulum, Mutant, Cell biology, 03 medical and health sciences, 030104 developmental biology, 0302 clinical medicine, 030220 oncology & carcinogenesis, Lipid biosynthesis, Chaperone (protein), biology.protein, Protein biosynthesis, Calreticulin, Peptide sequence, Calcium signaling
Abstract

The endoplasmic reticulum (ER) performs key cellular functions including protein synthesis, lipid metabolism and signaling. While these functions are spatially isolated in structurally distinct regions of the ER, there is cross-talk between the pathways. One vital player that is involved in ER function is the ER-resident protein calreticulin (CALR). It is a calcium ion-dependent lectin chaperone that primarily assists in glycoprotein synthesis in the ER as part of the protein quality control machinery. CALR also buffers calcium ion release and mediates other glycan-independent protein interactions. Mutations in CALR have been reported in a subset of chronic blood tumors called myeloproliferative neoplasms. The mutations consist of insertions or deletions in the CALR gene that all cause a + 1 bp shift in the reading frame and lead to a dramatic alteration of the amino acid sequence of the C-terminal domain of CALR. This alters CALR function and affects cell homeostasis. This chapter will discuss how CALR and mutant CALR affect ER health and disease.

Published
2021
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7. Platelet P-selectin initiates cross-presentation and dendritic cell differentiation in blood monocytes

Author

Patrick Han, Douglas Hanlon, Najla Arshad, Jung Seok Lee, Kazuki Tatsuno, Alp Yurter, Eve Robinson, Renata Filler, Olga Sobolev, Christine Cote, Felix Rivera-Molina, Derek Toomre, Tarek Fahmy, and Richard Edelson

Subjects
0303 health sciences, Multidisciplinary, P-selectin, Chemistry, Monocyte, Antigen presentation, Cross-presentation, Dendritic cell differentiation, In vitro, Calcium in biology, 3. Good health, Cell biology, 03 medical and health sciences, 0302 clinical medicine, medicine.anatomical_structure, medicine, Platelet, 030304 developmental biology, 030215 immunology
Abstract

Dendritic cells (DCs) are adept at cross-presentation and initiation of antigen-specific immunity. Clinically, however, DCs produced by in vitro differentiation of monocytes in the presence of exogenous cytokines have been met with limited success. We hypothesized that DCs produced in a physiological manner may be more effective and found that platelets activate a cross-presentation program in peripheral blood monocytes with rapid (18 hours) maturation into physiological DCs (phDCs). Differentiation of monocytes into phDCs was concomitant with the formation of an “adhesion synapse,” a biophysical junction enriched with platelet P-selectin and monocyte P-selectin glycoprotein ligand 1, followed by intracellular calcium fluxing and nuclear localization of nuclear factor κB. phDCs were more efficient than cytokine-derived DCs in generating tumor-specific T cell immunity. Our findings demonstrate that platelets mediate a cytokine-independent, physiologic maturation of DC and suggest a novel strategy for DC-based immunotherapies.

Published
2020
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8. Extracorporeal photochemotherapy induces bona fide immunogenic cell death

Author

Eve Robinson, Lorenzo Galluzzi, Olga Sobolev, Takahiro Yamazaki, Kazuki Tatsuno, Patrick Han, Alp Yurter, Najla Arshad, Richard L. Edelson, Felix Rivera-Molina, and Douglas Hanlon

Subjects
0301 basic medicine, Cancer Research, Apoptosis, Immunogenic Cell Death, Receptor, Interferon alpha-beta, CD8-Positive T-Lymphocytes, Monocytes, Mice, Adenosine Triphosphate, 0302 clinical medicine, Interferon, Leukocytes, HMGB1 Protein, Photosensitizing Agents, biology, lcsh:Cytology, Chemistry, Immune cell death, Cell Differentiation, Lymphoma, T-Cell, Cutaneous, Photopheresis, 030220 oncology & carcinogenesis, Tumour immunology, Methoxsalen, Immunogenic cell death, Antibody, medicine.drug, Cell death, Cell Survival, Ultraviolet Rays, Immunology, Article, 03 medical and health sciences, Cellular and Molecular Neuroscience, Antigen, Antigens, Neoplasm, Cell Line, Tumor, medicine, Animals, Humans, lcsh:QH573-671, Cutaneous T-cell lymphoma, Dendritic Cells, Cell Biology, medicine.disease, 030104 developmental biology, Cancer cell, biology.protein, Cancer research, Calreticulin, CD8
Abstract

Extracorporeal photochemotherapy (ECP) is employed for the management of cutaneous T cell lymphoma (CTCL). ECP involves the extracorporeal exposure of white blood cells (WBCs) to a photosensitizer, 8-methoxypsoralen (8-MOP), in the context of ultraviolet A (UVA) radiation, followed by WBC reinfusion. Historically, the therapeutic activity of ECP has been attributed to selective cytotoxicity on circulating CTCL cells. However, only a fraction of WBCs is exposed to ECP, and 8-MOP is inactive in the absence of UVA light, implying that other mechanisms underlie the anticancer effects of ECP. Recently, ECP has been shown to enable the physiological differentiation of monocytes into dendritic cells (DCs) that efficiently cross-present tumor-associated antigens (TAAs) to CD8+ T lymphocytes to initiate cognate immunity. However, the source of TAAs and immunostimulatory signals for such DCs remains to be elucidated. Here, we demonstrate that 8-MOP plus UVA light reduces melanoma cell viability along with the emission of ICD-associated danger signals including calreticulin (CALR) exposure on the cell surface and secretion of ATP, high mobility group box 1 (HMGB1) and type I interferon (IFN). Consistently, melanoma cells succumbing to 8-MOP plus UVA irradiation are efficiently engulfed by monocytes, ultimately leading to cross-priming of CD8+ T cells against cancer. Moreover, malignant cells killed by 8-MOP plus UVA irradiation in vitro vaccinate syngeneic immunocompetent mice against living cancer cells of the same type, and such a protection is lost when cancer cells are depleted of calreticulin or HMGB1, as well as in the presence of an ATP-degrading enzyme or antibodies blocking type I IFN receptors. ECP induces bona fide ICD, hence simultaneously providing monocytes with abundant amounts of TAAs and immunostimulatory signals that are sufficient to initiate cognate anticancer immunity.

Published
2019
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9. Tumor-associated calreticulin variants functionally compromise the peptide loading complex and impair its recruitment of MHC-I

Author

Peter Cresswell and Najla Arshad

Subjects
0301 basic medicine, genetic structures, Antigen presentation, Immunology, Peptide binding, Major histocompatibility complex, Biochemistry, 03 medical and health sciences, Neoplasms, MHC class I, Humans, cardiovascular diseases, Molecular Biology, Antigen Presentation, biology, Antigen processing, Chemistry, Endoplasmic reticulum, Histocompatibility Antigens Class I, Cell Biology, equipment and supplies, Peptide Fragments, Cell biology, 030104 developmental biology, Secretory protein, HEK293 Cells, Mutation, biology.protein, cardiovascular system, Calreticulin, circulatory and respiratory physiology, Signal Transduction
Abstract

Major histocompatibility complex-I–β(2)m dimers (MHC-I) bind peptides derived from intracellular proteins, enabling the immune system to distinguish between normal cells and those expressing pathogen-derived or mutant proteins. The peptides bind to MHC-I in the endoplasmic reticulum (ER), and this binding is facilitated by the peptide loading complex (PLC), which contains calreticulin (CRT). CRT associates with MHC-I via a conserved glycan present on MHC-I and recruits it to the PLC for peptide binding. Somatic frameshift mutations in CRT (CRT-FS) drive the proliferation of a subset of myeloproliferative neoplasms, which are chronic blood tumors. All CRT-FS proteins have a C-terminal sequence lacking the normal ER-retention signal and possessing a net negative charge rather than the normal positive charge. We characterized the effect of CRT-FS on antigen presentation by MHC-I in human cells. Our results indicate that CRT-FS cannot mediate CRT's peptide loading function in the PLC. Cells lacking CRT exhibited reduced surface MHC-I levels, consistent with reduced binding of high-affinity peptides, and this was not reversed by CRT-FS expression. CRT-FS was secreted and not detectably associated with the PLC, leading to poor MHC-I recruitment, although CRT-FS could still associate with MHC-I in a glycan-dependent manner. The addition of an ER-retention sequence to CRT-FS restored its association with the PLC but did not rescue MHC-I recruitment or its surface expression, indicating that the CRT-FS mutants functionally compromise the PLC. MHC-I down-regulation permits tumor cells to evade immune surveillance, and these findings may therefore be relevant for designing effective immunotherapies for managing myeloproliferative neoplasms.

Published
2018

10. The multiple and enigmatic roles of guanylyl cyclase C in intestinal homeostasis

Author

Sandhya S. Visweswariah and Najla Arshad

Subjects
Guanylyl cyclase C, medicine.medical_specialty, Receptors, Peptide, Guanylin, Biophysics, Receptors, Enterotoxin, Biology, Biochemistry, Mice, chemistry.chemical_compound, Immune system, Structural Biology, Internal medicine, Genetics, medicine, Animals, Homeostasis, Humans, Receptor, Cyclic GMP, Molecular Biology, Molecular Reproduction, Development & Genetics, Feeding Behavior, Cell Biology, Guanylate cyclase 2C, Intestine, Cell biology, Enzyme Activation, Intestines, cGMP, Endocrinology, Receptors, Guanylate Cyclase-Coupled, chemistry, Colonic Neoplasms, Intracellular, Uroguanylin, Hormone
Abstract

Guanylyl cyclase C (GC-C) is predominantly expressed in intestinal epithelial cells and serves as the receptor for the gastrointestinal hormones guanylin and uroguanylin, and the heat-stable enterotoxin, the causative agent for Travellers’ Diarrhea. Activation of GC-C results in an increase in intracellular levels of cGMP, which can regulate fluid and ion secretion, colon cell proliferation, and the gut immune system. This review highlights recent findings arising from studies in the GC-C knock-out mouse, along with enigmatic results obtained from the first descriptions of human disease caused by mutations in the GC-C gene. We provide some insight into these new findings and comment on areas of future study, which may enhance our knowledge of this evolutionarily conserved receptor and signaling system.

Published
2012
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11. Familial Diarrhea Syndrome Caused by an ActivatingGUCY2CMutation

Author

Torunn Fiskerstrand, Helge Boman, Jaran Apold, Khanh Pham, Siv L Tonder, Najla Arshad, Stefan Johansson, Rune Rose Tronstad, Sandhya S. Visweswariah, Nils Hovdenak, Bjørn Ivar Haukanes, Bjarte Håvik, Damien Brackman, Kabir H. Biswas, Shawn Levy, and Per M. Knappskog

Subjects
Diarrhea, Male, Heterozygote, medicine.medical_specialty, Receptors, Peptide, Genetic Linkage, Mutation, Missense, Receptors, Enterotoxin, medicine.disease_cause, Polymorphism, Single Nucleotide, Inflammatory bowel disease, Cystic fibrosis, Proinflammatory cytokine, Internal medicine, medicine, Humans, Missense mutation, Cyclic GMP, Exome sequencing, Mutation, business.industry, Heterozygote advantage, General Medicine, medicine.disease, Pedigree, Endocrinology, Receptors, Guanylate Cyclase-Coupled, Chronic Disease, Female, medicine.symptom, business, Signal Transduction
Abstract

BACKGROUND Familial diarrhea disorders are, in most cases, severe and caused by recessive mutations. We describe the cause of a novel dominant disease in 32 members of a Norwegian family. The affected members have chronic diarrhea that is of early onset, is relatively mild, and is associated with increased susceptibility to inflammatory bowel disease, small-bowel obstruction, and esophagitis. METHODS We used linkage analysis, based on arrays with single-nucleotide polymorphisms, to identify a candidate region on chromosome 12 and then sequenced GUCY2C, encoding guanylate cyclase C (GC-C), an intestinal receptor for bacterial heat-stable enterotoxins. We performed exome sequencing of the entire candidate region from three affected family members, to exclude the possibility that mutations in genes other than GUCY2C could cause or contribute to susceptibility to the disease. We carried out functional studies of mutant GC-C using HEK293T cells. RESULTS We identified a heterozygous missense mutation (c.2519G -> T) in GUCY2C in all affected family members and observed no other rare variants in the exons of genes in the candidate region. Exposure of the mutant receptor to its ligands resulted in markedly increased production of cyclic guanosine monophosphate (cGMP). This may cause hyperactivation of the cystic fibrosis transmembrane regulator (CFTR), leading to increased chloride and water secretion from the enterocytes, and may thus explain the chronic diarrhea in the affected family members. CONCLUSIONS Increased GC-C signaling disturbs normal bowel function and appears to have a proinflammatory effect, either through increased chloride secretion or additional effects of elevated cellular cGMP. Further investigation of the relevance of genetic variants affecting the GC-C-CFTR pathway to conditions such as Crohn's disease is warranted. (Funded by Helse Vest Western Norway Regional Health Authority] and the Department of Science and Technology, Government of India.)

Published
2012
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12. Receptor guanylyl cyclase C (GC-C): regulation and signal transduction

Author

Najla Arshad, Sandhya S. Visweswariah, and Nirmalya Basu

Subjects
Gastrointestinal tract, Receptors, Peptide, Guanylin, Clinical Biochemistry, Receptors, Enterotoxin, Cell Biology, General Medicine, Guanylate cyclase 2C, Biology, Gastrointestinal Tract, chemistry.chemical_compound, Receptors, Guanylate Cyclase-Coupled, Biochemistry, chemistry, Guanylate Cyclase, Animals, Humans, Tissue Distribution, Signal transduction, Receptor, Molecular Biology, Gene, Signal Transduction, Hormone, Uroguanylin
Abstract

Receptor guanylyl cyclase C (GC-C) is the target for the gastrointestinal hormones, guanylin, and uroguanylin as well as the bacterial heat-stable enterotoxins. The major site of expression of GC-C is in the gastrointestinal tract, although this receptor and its ligands play a role in ion secretion in other tissues as well. GC-C shares the domain organization seen in other members of the family of receptor guanylyl cyclases, though subtle differences highlight some of the unique features of GC-C. Gene knock outs in mice for GC-C or its ligands do not lead to embryonic lethality, but modulate responses of these mice to stable toxin peptides, dietary intake of salts, and development and differentiation of intestinal cells. It is clear that there is much to learn in future about the role of this evolutionarily conserved receptor, and its properties in intestinal and extra-intestinal tissues.

Published
2009
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13. Cyclic nucleotide signaling in intestinal epithelia: getting to the gut of the matter

Author

Najla Arshad and Sandhya S. Visweswariah

Subjects
Effector, Cell growth, Kinase, Medicine (miscellaneous), Biology, Adaptive Immunity, Biochemistry, Genetics and Molecular Biology (miscellaneous), Ion Channels, Receptors, G-Protein-Coupled, Cyclic nucleotide, chemistry.chemical_compound, chemistry, Biochemistry, Second messenger system, Cyclic AMP, Humans, Secretion, Signal transduction, Intestinal Mucosa, Phosphorus-Oxygen Lyases, Transcription factor, Cyclic GMP, Adenylyl Cyclases, Signal Transduction, Transcription Factors
Abstract

The intestine is the primary site of nutrient absorption, fluid-ion secretion, and home to trillions of symbiotic microbiota. The high turnover of the intestinal epithelia also renders it susceptible to neoplastic growth. These diverse processes are carefully regulated by an intricate signaling network. Among the myriad molecules involved in intestinal epithelial cell homeostasis are the second messengers, cyclic AMP (cAMP) and cyclic GMP (cGMP). These cyclic nucleotides are synthesized by nucleotidyl cyclases whose activities are regulated by extrinsic and intrinsic cues. Downstream effectors of cAMP and cGMP include protein kinases, cyclic nucleotide gated ion channels, and transcription factors, which modulate key processes such as ion-balance, immune response, and cell proliferation. The web of interaction involving the major signaling pathways of cAMP and cGMP in the intestinal epithelial cell, and possible cross-talk among the pathways, are highlighted in this review. Deregulation of these pathways occurs during infection by pathogens, intestinal inflammation, and cancer. Thus, an appreciation of the importance of cyclic nucleotide signaling in the intestine furthers our understanding of bowel disease, thereby aiding in the development of therapeutic approaches. WIREs Syst Biol Med 2013, 5:409–424. doi: 10.1002/wsbm.1223 Conflict of interest: The authors have declared no conflicts of interest for this article. For further resources related to this article, please visit the WIREs website.

Published
2013

14. Abstract A060: The effects of tumor-associated calreticulin mutants on antigen presentation

Author

Najla Arshad and Peter Cresswell

Subjects
Cancer Research, Immunology
Abstract

The phenomenon of antigen processing and presentation aids the immune system in distinguishing between normal and malignant cells. In cancer cells, Major Histocompatibility Complex (MHC) proteins present tumor- associated antigens (TAAs) that may serve as targets of immunotherapy. Antigen presentation by MHC class I-β2m heterodimers (MHC-I) requires peptide association to occur in in the ER. Binding is facilitated by the Peptide Loading Complex (PLC), which consists of the TAP transporter, tapasin, the thiol-oxidoreductase ERp57, and a lectin chaperone, calreticulin (CRT). CRT associates with MHC-I via the single, conserved, glycan present on MHC-I, drawing it into the PLC to facilitate peptide loading. CRT is comprised of an N-terminal lectin domain, a proline-rich central P domain, and a negatively charged C-terminal domain (CTD) that is also contains an ER retention motif. Two recent studies report a mutant CRT associated with myeloproliferative neoplasms (MPNs). These MPNs carry a somatic frame-shift CRT mutation (CRTFS) that generates a novel CTD that lacks the ER-retention signal and renders it positively charged. Previous studies have shown that ablation of CRT expression in mouse embryonic fibroblast cells result in decreased surface expression of MHC-I, which is reversed on reconstitution of full-length CRT. Interestingly, reconstitution of CRT lacking the CTD did not restore MHC-I expression, indicating a role for the CTD in MHC-I expression. We therefore suspect that antigen presentation in MPNs carrying the CRTFS is altered. To address the role of CRTFS in antigen presentation in a human cell line, we have generated a CRT knockout of HEK293T cells using CRISPR/Cas9 technology. The CRT−/− cells exhibit reduced surface levels of MHC-I. We used these calreticulin-deficient cells to generate stable cell lines expressing CRT or CRTFS. We find that expression of CRT restores surface MHC-I, but expression of CRTFS does not. We are currently assessing the reason behind the alterations in MHC-I expression in these cell lines using various biochemical techniques. Future experiments include analysis of the peptide repertoire displayed on the surface of these cells as well as changes in the molecular interactions of the mutant CRT with other members of the PLC. After a preliminary study in HEK293T cells, we will study the effect of CRTFS in antigen presentation in MPN cell lines to identify unique TAAs to facilitate the specific targeting of these cells by immunotherapy. Citation Format: Najla Arshad, Peter Cresswell. The effects of tumor-associated calreticulin mutants on antigen presentation [abstract]. In: Proceedings of the Second CRI-CIMT-EATI-AACR International Cancer Immunotherapy Conference: Translating Science into Survival; 2016 Sept 25-28; New York, NY. Philadelphia (PA): AACR; Cancer Immunol Res 2016;4(11 Suppl):Abstract nr A060.

Published
2016
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15. Site-specific N-Linked Glycosylation of Receptor Guanylyl Cyclase C Regulates Ligand Binding, Ligand-mediated Activation and Interaction with Vesicular Integral Membrane Protein 36, VIP36*

Author

Najla Arshad, Suhas Ballal, and Sandhya S. Visweswariah

Subjects
Protein Folding, Glycosylation, genetic structures, Receptors, Peptide, Guanylin, Glycobiology and Extracellular Matrices, Receptors, Enterotoxin, Plasma protein binding, Biology, Endoplasmic Reticulum, Ligands, Biochemistry, Cell Line, Gastrointestinal Hormones, chemistry.chemical_compound, N-linked glycosylation, Humans, Natriuretic Peptides, Molecular Biology, Integral membrane protein, Cell Membrane, Membrane Transport Proteins, Cell Biology, Guanylate cyclase 2C, Ligand (biochemistry), Protein Structure, Tertiary, carbohydrates (lipids), Mannose-Binding Lectins, chemistry, Receptors, Guanylate Cyclase-Coupled, sense organs, Uroguanylin, Protein Binding
Abstract

Guanylyl cyclase C (GC-C) is a multidomain, membrane-associated receptor guanylyl cyclase. GC-C is primarily expressed in the gastrointestinal tract, where it mediates fluid-ion homeostasis, intestinal inflammation, and cell proliferation in a cGMP-dependent manner, following activation by its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST). GC-C is also expressed in neurons, where it plays a role in satiation and attention deficiency/hyperactive behavior. GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity. When glycosylation of human GC-C was prevented, either by pharmacological intervention or by mutation of all of the 10 predicted glycosylation sites, ST binding and surface localization was abolished. Systematic mutagenesis of each of the 10 sites of glycosylation in GC-C, either singly or in combination, identified two sites that were critical for ligand binding and two that regulated ST-mediated activation. We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36. Interaction with VIP36 is dependent on glycosylation at the same sites that allow GC-C to fold and bind ligand. Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.

Published
2012

16. G Protein Alpha 12

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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17. Gastric Inhibitory Polypeptide Receptor

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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18. G-Protein αq (Gene Name: GNAQ)

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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19. GPCR84

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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20. Grp94 (HSP90B1)

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Subjects
endoplasmic reticulum, CELL SURFACE, Molecular chaperone, signal transduction
Published
2012

21. Gz Alpha Subunit

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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22. Gsto 1

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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23. GPSM3/G-Protein Signaling Modulator 3/G18/NG1 (AGS4)

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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24. Guanine Nucleotide Binding Protein, Alpha o

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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25. Glucose-Dependent Insulinotropic Polypeptide Receptor (GIPR)

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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26. GC-B

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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27. GC-G

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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28. Guanylyl Cyclase

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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29. GC-D

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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30. Guanine Nucleotide Exchange Factor, Calcium- and DAG-Regulated

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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31. Guanylyl Cyclase Receptors

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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32. GALR, Galanin Receptor

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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33. GPSM2/G-Protein Signaling Modulator 2/LGN/mPINS (AGS5)

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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34. GATA-Binding Protein 3

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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35. Guanine Nucleotide Exchange Factor

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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36. G Alpha (o)

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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37. G Protein α i

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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38. G Protein α z

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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39. GNAO /Gαo/Guanine Nucleotide Binding Protein/Alpha Activating Activity Polypeptide O (AGS10)

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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40. G Protein α o

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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41. G Protein Alpha i

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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42. Guanine Nucleotide Binding Protein (G Protein), Gamma

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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43. GAT-2

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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44. GATA-3 (GATA Binding Protein 3)

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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45. Guanine Nucleotide Binding Protein, Beta

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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46. GAL-R

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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47. GEFT, p63RhoGEF

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
Full Text
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48. G Protein Beta/Gamma

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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49. Glutathione-S-Transferases: As Signaling Molecules

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
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50. GAT (GABA Transporters)

Author

Thomas E. Meigs, Alex Lyakhovich, Hoon Shim, Ching-Kang Chen, Denis J. Dupré, Terence E. Hébert, Joe B. Blumer, Gregory G. Tall, Richard Vaillancourt, Annina C. Spilker, Morag Park, Yongping Wang, Haihua Gu, Mikko Uusi-Oukari, Joshua D. Brown-Clay, Albert J. Fornace, Zhenhui Liu, Linfang Li, Min Zhang, Sergei Krirschuk, Werner Kilb, Anuradha Ray, Anupriya Khare, Nandini Krishnamoorthy, Prabir Ray, Karl-Wilhelm Koch, Rakesh Chandarana, Jacinta S. D’Souza, Evans C. Coutinho, Elek Molnár, Thyaga Raju Kedam, Pallavi Chittoor, Divya Kurumala, James Woodgett, Kimberly J. Perry, Jonathan J. Henry, Björn H. Falkenburger, Frank S. Chen, Luisa Gorza, Maurizio Vitadello, Nirmalya Basu, Sandhya S. Visweswariah, and Najla Arshad

Published
2012
Full Text
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