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Your search keyword '"Lussier, Marc"' showing total 167 results
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167 results on '"Lussier, Marc"'

1. AP-1 contributes to endosomal targeting of the ubiquitin ligase RNF13 via a secondary and novel non-canonical binding motif.

Author

Cabana, Valérie C., Séncal, Audrey M., Bouchard, Antoine Y., Kourrich, Saïd, Cappadocia, Laurent, and Lussier, Marc P.

Subjects
CARRIER proteins, UBIQUITIN ligases, CLATHRIN, UBIQUITIN, HELA cells
Abstract

Cellular trafficking between organelles is typically assured by short motifs that contact carrier proteins to transport them to their destination. The ubiquitin E3 ligase RING finger protein 13 (RNF13), a regulator of proliferation, apoptosis and protein trafficking, localizes to endolysosomal compartments through the binding of a dileucine motif to clathrin adaptor protein complex AP-3. Mutations within this motif reduce the ability ofRNF13 to interactwithAP-3. Here, our study shows the discovery of a glutamine-based motif that resembles a tyrosinebased motif within the C-terminal region of RNF13 that binds to the clathrin adaptor protein complex AP-1, notably without a functional interaction with AP-3. Using biochemical, molecular and cellular approaches in HeLa cells, our study demonstrates that a RNF13 dileucine variant uses anAP-1-dependent pathway to be exported from the Golgi towards the endosomal compartment. Overall, this study provides mechanistic insights into the alternate route used by this variant of the dileucine sorting motif of RNF13. [ABSTRACT FROM AUTHOR]

Published
2024
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3. The neuro genomics partnership: A new consortium dedicated to a fully open patient to patient (P2P) integrative R&D approach

Author

Degroot, Clotilde, primary, Taylor, Kirsten, additional, Mooser, Vincent, additional, Rouleau, Guy, additional, Gan-Or, Ziv, additional, Sharp, Madeleine, additional, Durcan, Thomas, additional, Postuma, Ronald, additional, Doyon, Julien, additional, Kustermann, Thomas, additional, Jagasia, Ravi, additional, Taylor, Caitlin, additional, Lussier, Marc, additional, and Fon, Edward, additional

Published
2023
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4. Ubiquitin ligase RNF167 regulates AMPA receptor-mediated synaptic transmission

Author

Lussier, Marc P, Herring, Bruce E, Nasu-Nishimura, Yukiko, Neutzner, Albert, Karbowski, Mariusz, Youle, Richard J, Nicoll, Roger A, and Roche, Katherine W

Subjects
Neurosciences, Mental Health, Genetics, Underpinning research, 1.1 Normal biological development and functioning, Neurological, Animals, Cells, Cultured, Gene Expression Regulation, Gene Knockdown Techniques, HeLa Cells, Hippocampus, Humans, Lysosomes, Neurons, Protein Transport, RNA, Messenger, Rats, Rats, Sprague-Dawley, Receptors, AMPA, Synaptic Transmission, Ubiquitin-Protein Ligases, Ubiquitination, hippocampus, glutamate receptor, GluA2, Hela Cells
Abstract

AMPA receptors (AMPARs) mediate the majority of fast excitatory neurotransmission, and their density at postsynaptic sites determines synaptic strength. Ubiquitination is a posttranslational modification that dynamically regulates the synaptic expression of many proteins. However, very few of the ubiquitinating enzymes implicated in the process have been identified. In a screen to identify transmembrane RING domain-containing E3 ubiquitin ligases that regulate surface expression of AMPARs, we identified RNF167. Predominantly lysosomal, a subpopulation of RNF167 is located on the surface of cultured neurons. Using a RING mutant RNF167 or a specific shRNA to eliminate endogenous RNF167, we demonstrate that AMPAR surface expression increases in hippocampal neurons with disrupted RNF167 activity and that RNF167 is involved in activity-dependent ubiquitination of AMPARs. In addition, RNF167 regulates synaptic AMPAR currents, whereas synaptic NMDAR currents are unaffected. Therefore, our study identifies RNF167 as a selective regulator of AMPAR-mediated neurotransmission and expands our understanding of how ubiquitination dynamically regulates excitatory synapses.

Published
2012

5. Functional Characterization of the S. cerevisiae Genome by Gene Deletion and Parallel Analysis

Author

Winzeler, Elizabeth A., Shoemaker, Daniel D., Astromoff, Anna, Liang, Hong, Anderson, Keith, Andre, Bruno, Bangham, Rhonda, Benito, Rocio, Boeke, Jef D., Bussey, Howard, Chu, Angela M., Connelly, Carla, Davis, Karen, Dietrich, Fred, Dow, Sally Whelen, El Bakkoury, Mohamed, Foury, Franco̧ise, Friend, Stephen H., Gentalen, Erik, Giaever, Guri, Hegemann, Johannes H., Jones, Ted, Laub, Michael, Liao, Hong, Liebundguth, Nicole, Lockhart, David J., Lucau-Danila, Anca, Lussier, Marc, Menard, Patrice, Mittmann, Michael, Pai, Chai, Rebischung, Corinne, Revuelta, Jose L., Riles, Linda, Roberts, Christopher J., Ross-MacDonald, Petra, Scherens, Bart, Snyder, Michael, Sookhai-Mahadeo, Sharon, Storms, Reginald K., Véronneau, Steeve, Voet, Marleen, Volckaert, Guido, Ward, Teresa R., Wysocki, Robert, Yen, Grace S., Yu, Kexin, Zimmermann, Katja, Philippsen, Peter, Johnston, Mark, and Davis, Ronald W.

Published
1999

19. Functional profiling of the Saccharomyces cerevisiae genome

Author

Giaever, Guri, Chu, Angela M., Ni, Li, Connelly, Carla, Riles, Linda, Véronneau, Steeve, Dow, Sally, Lucau-Danila, Ankuta, Anderson, Keith, André, Bruno, Arkin, Adam P., Astromoff, Anna, El Bakkoury, Mohamed, Bangham, Rhonda, Benito, Rocio, Brachat, Sophie, Campanaro, Stefano, Curtiss, Matt, Davis, Karen, Deutschbauer, Adam, Entian, Karl-Dieter, Flaherty, Patrick, Foury, Francoise, Garfinkel, David J., Gerstein, Mark, Gotte, Deanna, Güldener, Ulrich, Hegemann, Johannes H., Hempel, Svenja, Herman, Zelek, Jaramillo, Daniel F., Kelly, Diane E., Kelly, Steven L., Kötter, Peter, LaBonte, Darlene, Lamb, David C., Lan, Ning, Liang, Hong, Liao, Hong, Liu, Lucy, Luo, Chuanyun, Lussier, Marc, Mao, Rong, Menard, Patrice, Ooi, Siew Loon, Revuelta, Jose L., Roberts, Christopher J., Rose, Matthias, Ross-Macdonald, Petra, Scherens, Bart, Schimmack, Greg, Shafer, Brenda, Shoemaker, Daniel D., Sookhai-Mahadeo, Sharon, Storms, Reginald K., Strathern, Jeffrey N., Valle, Giorgio, Voet, Marleen, Volckaert, Guido, Wang, Ching-yun, Ward, Teresa R., Wilhelmy, Julie, Winzeler, Elizabeth A., Yang, Yonghong, Yen, Grace, Youngman, Elaine, Yu, Kexin, Bussey, Howard, Boeke, Jef D., Snyder, Michael, Philippsen, Peter, Davis, Ronald W., and Johnston, Mark

Published
2002
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22. Isolation of Candida glabrata homologs of the Saccharomyces cerevisiae KRE9 and KNH1 genes and their involvement in cell wall beta-1,6-glucan synthesis

Author

Nagahashi, Shigehisa, Lussier, Marc, and Bussey, Howard

Subjects
Candida -- Genetic aspects, Saccharomyces -- Genetic aspects, Glucans -- Research, Bacterial cell walls -- Research, Yeast fungi -- Genetic aspects, Biological sciences
Abstract

The Candida glabrata (CgKRE9) and KNH1 (CgKNH1) genes were isolated as multicopy suppressors of the tetracycline-responsive growth of a Saccharomyces cerevisiae mutant with the damaged KNH1 locus and the KRE9 gene regulated by a tetracycline-sensitive promoter. Disruption of CgKRE9 resulted in several phenotypes similar to those of the S. cerevisiae kre9-delta null mutant, massive growth defect on glucose medium, resistance to the K1 killer toxin, a 50% decrease in beta-1,6-glucan and the presence of groups of cells with abnormal morphology on glucose medium.

Published
1998

23. The Candida albicans KRE9 gene is required for cell wall beta-1,6-glucan synthesis and is essential for growth on glucose

Author

Lussier, Marc, Sdicu, Anne-Marie, Shahinian, Serge, and Bussey, Howard

Subjects
Candida albicans -- Genetic aspects, Bacterial cell walls -- Research, Glucans -- Research, Glucose -- Synthesis, Science and technology
Abstract

We have isolated CaKRE9, a gene from Candida albicans, that is a functional homologue of the Saccharomyces cerevisiae KRE9 gene involved in [Beta]-1,6-glucan synthesis. Disruption of the CaKRE9 gene in C. albicans shows that CaKre9p is required for the synthesis or assembly of this fungal polymer. Homozygous null disruptants of CaKRE9 grow poorly on galactose and fail to form hyphae in serum, and, in growth medium containing glucose, the gene is essential. Thus, the CaKRE9 gene product is a potentially useful candidate as a target for fungal-specific drugs.

Published
1998

24. Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae

Author

Lussier, Marc, White, Ann-Marie, Sheraton, Jane, Di Paolo, Tiziano, Treadwell, Julie, Southard, Susan B., Horenstein, Craig I., Chen-Weiner, Joan, Ram, Arthur F.J., Kapteyn, Johan C., Roemer, Terry W., Vo. Dahn H., Bondoc, Dana C., Hall, John, Zhong, Wu Wei, Sdicu, Anne-Marie, Davies, Julian, Klis, Frans M., Robbins, Phillips W., and Bussey, Howard

Subjects
Saccharomyces -- Genetic aspects, Gene mutations -- Research, Biosynthesis -- Research, Plasma membranes -- Research, Biological sciences
Abstract

The sequenced yeast genome offers a unique resource for the analysis of eukaryotic cell function and enables genome-wide screens for genes involved in cellular processes. We have identified genes involved in cell surface assembly by screening transposon-mutagenized cells for altered sensitivity to calcofluor white, followed by supplementary screens to further characterize mutant phenotypes. The mutated genes were directly retrieved from genomic DNA and then matched uniquely to a gene in the yeast genome database. Eighty-two genes with apparent perturbation of the cell surface were identified, with mutations in 65 of them displaying at least one further cell surface phenotype in addition to their modified sensitivity to calcofluor. Fifty of these genes were previously known, 17 encoded proteins whose function could be anticipated through sequence homology or previously recognized phenotypes and 15 genes had no previously known phenotype.

Published
1997

26. Localization and targeting of the Saccharomyces cerevisiae Kre2p/Mnt1p alpha-1,2-mannosyltransferase to a medial-Golgi compartment

Author

Lussier, Marc, Sdicu, Anne-Marie, Ketela, Troy, and Bussey, Howard

Subjects
Saccharomyces -- Research, Membrane proteins -- Research, Golgi apparatus -- Observations, Proteins -- Conformation, Biological sciences
Abstract

The correct localization of the Saccharomyces cerevisiae Kre2p/Mnt1p alpha-1,2-mannosyltransferase membrane protein in the Golgi body requires the short NH2-terminal cytoplasmic tail domain of Kre2p. The membrane spanning and the stem regions of the Kre2p protein are not necessary for this process. The Kre2p protein is localized in a Golgi compartment that extends over the compartment containing the medial-Golgi mannosyltransferase Mnn1p. The Kre2p/Mnt1p protein has a type II orientation that is N-glycosylated in an MNNI-dependent fashion.

Published
1995

28. Keratin 19 as a biochemical marker of skin stem cells in vivo and in vitro: keratin 19 expressing cells are differentially localized in function of anatomic sites, and their number varies with donor age and culture stage

Author

Török, Natalie, Michel, Martine, Germain, Lucie, Lussier, Marc, Godbout, Marie-Josée, Gaudreau, Pierrette, Royal, André, Török, Natalie, Michel, Martine, Germain, Lucie, Lussier, Marc, Godbout, Marie-Josée, Gaudreau, Pierrette, and Royal, André

Abstract

This study was undertaken to evaluate keratin 19 (K19) as a biochemical marker for skin stem cells in order to address some long standing questions concerning these cells in the field of cutaneous biology. We first used the well-established mouse model enabling us to identify skin stem cells as [3H]thymidine-label-retaining cells. A site directed antibody was raised against a synthetic peptide of K19. It reacted specifically with a 40 kDa protein (K19) on immunoblotting. It labelled the bulge area of the outer root sheath on mouse skin by immunohistochemistry. Double-labelling revealed that K19-positive-cells were also [3H]thymidine-label-retaining cells, suggesting that K19 is a marker for skin stem cells of hair follicles. K19-expression was then used to investigate the variation in mouse and human skin stem cells as a function of body site, donor age and culture time. K19 was expressed in the hair follicle and absent from the interfollicular epidermis at hairy sites (except for some K18 coexpressing Merkel cells). In contrast, at glabrous sites, K19-positive-cells were in deep epidermal rete ridges. K19 expressing cells also contained high levels of alpha 3 beta 1 integrin. The proportion of K19-positive-cells was greater in newborn than older foreskins. This correlated with keratinocyte culture lifespan variation with donor age. Moreover, it could explain clinical observations that children heal faster than adults. In conclusion, K19 expression in skin provides an additional tool to allow further characterization of skin stem cells under normal and pathological conditions in situ and in vitro.

Published
2018

31. Classification: Molecular & Synaptic Mechanisms: Casein kinase 2 phosphorylates GluA1 and regulates its surface expression

Author

Lussier, Marc P., Gu, Xinglong, Lu, Wei, and Roche, Katherine W.

Subjects
Cerebral Cortex, Neurons, Cell Membrane, Molecular Sequence Data, Hippocampus, Article, Protein Structure, Tertiary, Rats, Rats, Sprague-Dawley, Mice, Protein Transport, HEK293 Cells, Animals, Humans, Amino Acid Sequence, Receptors, AMPA, Phosphorylation, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Casein Kinase II, Cells, Cultured
Abstract

Controlling the density of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs) at synapses is essential for regulating the strength of excitatory neurotransmission. In particular, the phosphorylation of AMPARs is important for defining both synaptic expression and intracellular routing of receptors. Phosphorylation is a post-translational modification known to regulate many cellular events and the C-termini of glutamate receptors are important targets. Recently, the first intracellular loop1 region of the GluA1 subunit of AMPARs was reported to regulate synaptic targeting through phosphorylation of S567 by Ca2+ /calmodulin-dependent protein kinase II (CaMKII). Intriguingly, the loop1 region of all four AMPAR subunits contains many putative phosphorylation sites (S/T/Y), leaving the possibility that other kinases may regulate AMPAR surface expression via phosphorylation of the loop regions. To explore this hypothesis, we used in vitro phosphorylation assays with a small panel of purified kinases and found that casein kinase 2 (CK2) phosphorylates the GluA1 and GluA2 loop1 regions, but not GluA3 or GluA4. Interestingly, when we reduced the endogenous expression of CK2 using a specific short hairpin RNA against the regulatory subunit CK2β, we detected a reduction of GluA1 surface expression, whereas GluA2 was unchanged. Furthermore, we identified S579 of GluA1 as a substrate of CK2, and the expression of GluA1 phosphodeficient mutants in hippocampal neurons displayed reduced surface expression. Therefore, our study identifies CK2 as a regulator of GluA1 surface expression by phosphorylating the intracellular loop1 region.

Published
2014

33. Identification et caractérisation de nouveaux partenaires d'intéraction liant le domaine de répétitions similaires à l'ankyrine des TRPCs

Author

Lussier, Marc, [non identifié], Lussier, Marc, and [non identifié]

Abstract

Le Ca[exposant]2+ joue un rôle majeur dans la régulation de processus physiologiques et biochimiques de l'organisme. Chez les cellules non-excitables, les TRPCs (transient receptor potential canonical) sont des canaux calciques impliqués dans l'influx de Ca[exposant]2+ à la membrane plasmique. Bien que de nombreux efforts soient déployés, le mécanisme régulant l'activité et le routage des TRPCs est encore mal connu. Au cours des dernières années, l'étude de domaines conservés au sein des protéines a connu un engouement. Tous les TRPCs possèdent un domaine de répétitions similaires à l'ankyrine (ANK), un motif bien connu pour son implication dans des interactions protéine-protéine. Le but de la présente étude était d'identifier de nouveaux partenaires d'interaction du domaine ANK des TRPCs. Pour ce faire, nous avons utilisé l'approche de double-hybride chez la levure afin de cribler une librairie d'ADNc, ce qui nous a permis d'identifier MxA et RNF24. MxA est une protéine faisant partie de la superfamille de la dynamine. Elle possède plusieurs propriétés de la dynamine classique, dont celle d'oligomériser. La première partie de l'étude démontre que MxA interagit au niveau de la deuxième répétition similaire à l'ankyrine de TRPC6 et que cette protéine peut lier tour les TRPCs, autant in vitro qu'in cellulo. Des mesures de Ca[exposant]2+ intracellulaire effectuées sur des cellules HEK 293T démontrent que l'interaction entre MxA et TRPC6 modifie significativement l'activité de TRPC6. De plus, l'utilisation de mutants de MxA démontre que la modulation de l'activité de TRPC6 s'effectue lorsque MxA est sous sa forme monomérique liée au GTP. Les résultats démontrent que MxA lie le domaine ANK de TRPC6 et modifie son activité. La découverte de RNF24 a permis d'identifier une nouvelle protéine membranaire localisée au niveau de l'appareil de Golgi. L'expression de RNF24 réduit spécifiquement l'insertion des TRPCs a la membrane plasmique, cause une rétention intracellulaire de

Published
2008

35. Functional profiling of the Saccharomyces cerevisiae genome.

Author

UCL - SST/ISV - Institut des sciences de la vie, Giaever, Guri, Chu, Angela M, Ni, Li, Connelly, Carla, Riles, Linda, Véronneau, Steeve, Dow, Sally, Lucau-Danila, Ankuta, Anderson, Keith, André, Bruno, Arkin, Adam P, Astromoff, Anna, El-Bakkoury, Mohamed, Bangham, Rhonda, Benito, Rocio, Brachat, Sophie, Campanaro, Stefano, Curtiss, Matt, Davis, Karen, Deutschbauer, Adam, Entian, Karl-Dieter, Flaherty, Patrick, Foury, Françoise, Garfinkel, David J, Gerstein, Mark, Gotte, Deanna, Güldener, Ulrich, Hegemann, Johannes H, Hempel, Svenja, Herman, Zelek, Jaramillo, Daniel F, Kelly, Diane E, Kelly, Steven L, Kötter, Peter, LaBonte, Darlene, Lamb, David C, Lan, Ning, Liang, Hong, Liao, Hong, Liu, Lucy, Luo, Chuanyun, Lussier, Marc, Mao, Rong, Menard, Patrice, Ooi, Siew Loon, Revuelta, Jose L, Roberts, Christopher J, Rose, Matthias, Ross-Macdonald, Petra, Scherens, Bart, Schimmack, Greg, Shafer, Brenda, Shoemaker, Daniel D, Sookhai-Mahadeo, Sharon, Storms, Reginald K, Strathern, Jeffrey N, Valle, Giorgio, Voet, Marleen, Volckaert, Guido, Wang, Ching-yun, Ward, Teresa R, Wilhelmy, Julie, Winzeler, Elizabeth A, Yang, Yonghong, Yen, Grace, Youngman, Elaine, Yu, Kexin, Bussey, Howard, Boeke, Jef D, Snyder, Michael, Philippsen, Peter, Davis, Ronald W, Johnston, Mark, UCL - SST/ISV - Institut des sciences de la vie, Giaever, Guri, Chu, Angela M, Ni, Li, Connelly, Carla, Riles, Linda, Véronneau, Steeve, Dow, Sally, Lucau-Danila, Ankuta, Anderson, Keith, André, Bruno, Arkin, Adam P, Astromoff, Anna, El-Bakkoury, Mohamed, Bangham, Rhonda, Benito, Rocio, Brachat, Sophie, Campanaro, Stefano, Curtiss, Matt, Davis, Karen, Deutschbauer, Adam, Entian, Karl-Dieter, Flaherty, Patrick, Foury, Françoise, Garfinkel, David J, Gerstein, Mark, Gotte, Deanna, Güldener, Ulrich, Hegemann, Johannes H, Hempel, Svenja, Herman, Zelek, Jaramillo, Daniel F, Kelly, Diane E, Kelly, Steven L, Kötter, Peter, LaBonte, Darlene, Lamb, David C, Lan, Ning, Liang, Hong, Liao, Hong, Liu, Lucy, Luo, Chuanyun, Lussier, Marc, Mao, Rong, Menard, Patrice, Ooi, Siew Loon, Revuelta, Jose L, Roberts, Christopher J, Rose, Matthias, Ross-Macdonald, Petra, Scherens, Bart, Schimmack, Greg, Shafer, Brenda, Shoemaker, Daniel D, Sookhai-Mahadeo, Sharon, Storms, Reginald K, Strathern, Jeffrey N, Valle, Giorgio, Voet, Marleen, Volckaert, Guido, Wang, Ching-yun, Ward, Teresa R, Wilhelmy, Julie, Winzeler, Elizabeth A, Yang, Yonghong, Yen, Grace, Youngman, Elaine, Yu, Kexin, Bussey, Howard, Boeke, Jef D, Snyder, Michael, Philippsen, Peter, Davis, Ronald W, and Johnston, Mark

Abstract

Determining the effect of gene deletion is a fundamental approach to understanding gene function. Conventional genetic screens exhibit biases, and genes contributing to a phenotype are often missed. We systematically constructed a nearly complete collection of gene-deletion mutants (96% of annotated open reading frames, or ORFs) of the yeast Saccharomyces cerevisiae. DNA sequences dubbed 'molecular bar codes' uniquely identify each strain, enabling their growth to be analysed in parallel and the fitness contribution of each gene to be quantitatively assessed by hybridization to high-density oligonucleotide arrays. We show that previously known and new genes are necessary for optimal growth under six well-studied conditions: high salt, sorbitol, galactose, pH 8, minimal medium and nystatin treatment. Less than 7% of genes that exhibit a significant increase in messenger RNA expression are also required for optimal growth in four of the tested conditions. Our results validate the yeast gene-deletion collection as a valuable resource for functional genomics.

Published
2002

38. Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis.

Author

Winzeler, Elizabeth A, Shoemaker, Daniel D, Astromoff, Anna, Liang, Hong, Anderson, Keith, André, Bruno, Bangham, Rhonda, Benito, Rocio, Boeke, Jef D, Bussey, Howard, Chu, Angela M, Connelly, Carla, Davis, Karen, Dietrich, F, Dow, Sally, El Bakkoury, Mohamed, Foury, Francoise, Friend, S H, Gentalen, E, Giaever, Guri, Hegemann, Johannes H, Jones, T.C., Laub, M, Liao, Hong, Liebundguth, N, Lockhart, D. J., Lucau-Danila, Ankuta, Lussier, Marc, M'Rabet, Nasiha, Menard, Patrice, Mittmann, M, Pai, C, Rebischung, C, Revuelta, Jose L, Riles, Linda, Roberts, Christopher J, Ross, M., Scherens, Bart, Snyder, Mark, Sookhai-Mahadeo, Sharon, Storms, Reginald K, Véronneau, Steeve, Voet, Marleen, Volckaert, Guido, Ward, Teresa R, Wysocki, R, Yen, Grace, Yu, Keming, Zimmermann, Klaus, Philippsen, Peter, Johnston, Mark, Davis, Ronald W, Winzeler, Elizabeth A, Shoemaker, Daniel D, Astromoff, Anna, Liang, Hong, Anderson, Keith, André, Bruno, Bangham, Rhonda, Benito, Rocio, Boeke, Jef D, Bussey, Howard, Chu, Angela M, Connelly, Carla, Davis, Karen, Dietrich, F, Dow, Sally, El Bakkoury, Mohamed, Foury, Francoise, Friend, S H, Gentalen, E, Giaever, Guri, Hegemann, Johannes H, Jones, T.C., Laub, M, Liao, Hong, Liebundguth, N, Lockhart, D. J., Lucau-Danila, Ankuta, Lussier, Marc, M'Rabet, Nasiha, Menard, Patrice, Mittmann, M, Pai, C, Rebischung, C, Revuelta, Jose L, Riles, Linda, Roberts, Christopher J, Ross, M., Scherens, Bart, Snyder, Mark, Sookhai-Mahadeo, Sharon, Storms, Reginald K, Véronneau, Steeve, Voet, Marleen, Volckaert, Guido, Ward, Teresa R, Wysocki, R, Yen, Grace, Yu, Keming, Zimmermann, Klaus, Philippsen, Peter, Johnston, Mark, and Davis, Ronald W

Abstract

The functions of many open reading frames (ORFs) identified in genome-sequencing projects are unknown. New, whole-genome approaches are required to systematically determine their function. A total of 6925 Saccharomyces cerevisiae strains were constructed, by a high-throughput strategy, each with a precise deletion of one of 2026 ORFs (more than one-third of the ORFs in the genome). Of the deleted ORFs, 17 percent were essential for viability in rich medium. The phenotypes of more than 500 deletion strains were assayed in parallel. Of the deletion strains, 40 percent showed quantitative growth defects in either rich or minimal medium., Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S., SCOPUS: ar.j, info:eu-repo/semantics/published

Published
1999

39. Keratin 19 as a biochemical marker of skin stem cells in vivo and in vitro: keratin 19 expressing cells are differentially localized in function of anatomic sites, and their number varies with donor age and culture stage

Author

Michel, Martine, Török, Natalie, Godbout, Marie-Josée, Lussier, Marc, Gaudreau, Pierrette, Royal, André, Germain, Lucie, Michel, Martine, Török, Natalie, Godbout, Marie-Josée, Lussier, Marc, Gaudreau, Pierrette, Royal, André, and Germain, Lucie

Abstract

This study was undertaken to evaluate keratin 19 (K19) as a biochemical marker for skin stem cells in order to address some long standing questions concerning these cells in the field of cutaneous biology. We first used the well-established mouse model enabling us to identify skin stem cells as [3H]thymidine-label-retaining cells. A site directed antibody was raised against a synthetic peptide of K19. It reacted specifically with a 40 kDa protein (K19) on immunoblotting. It labelled the bulge area of the outer root sheath on mouse skin by immunohistochemistry. Double-labelling revealed that K19-positive-cells were also [3H]thymidine-label-retaining cells, suggesting that K19 is a marker for skin stem cells of hair follicles. K19-expression was then used to investigate the variation in mouse and human skin stem cells as a function of body site, donor age and culture time. K19 was expressed in the hair follicle and absent from the interfollicular epidermis at hairy sites (except for some K18 coexpressing Merkel cells). In contrast, at glabrous sites, K19-positive-cells were in deep epidermal rete ridges. K19 expressing cells also contained high levels of alpha 3 beta 1 integrin. The proportion of K19-positive-cells was greater in newborn than older foreskins. This correlated with keratinocyte culture lifespan variation with donor age. Moreover, it could explain clinical observations that children heal faster than adults. In conclusion, K19 expression in skin provides an additional tool to allow further characterization of skin stem cells under normal and pathological conditions in situ and in vitro.

Published
1996

40. Casein kinase 2 phosphorylates Glu A1 and regulates its surface expression.

Author

Lussier, Marc P., Gu, Xinglong, Lu, Wei, and Roche, Katherine W.

Subjects
*PROTEIN kinase CK2, *PHOSPHORYLATION, *GENETIC regulation, *GLUTAMIC acid, *AMPA receptors, *NEURAL transmission, *GLUTAMATE receptors
Abstract

Controlling the density of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors ( AMPARs) at synapses is essential for regulating the strength of excitatory neurotransmission. In particular, the phosphorylation of AMPARs is important for defining both synaptic expression and intracellular routing of receptors. Phosphorylation is a post-translational modification known to regulate many cellular events and the C-termini of glutamate receptors are important targets. Recently, the first intracellular loop1 region of the Glu A1 subunit of AMPARs was reported to regulate synaptic targeting through phosphorylation of S567 by Ca2+/calmodulin-dependent protein kinase II ( Ca MKII). Intriguingly, the loop1 region of all four AMPAR subunits contains many putative phosphorylation sites ( S/ T/ Y), leaving the possibility that other kinases may regulate AMPAR surface expression via phosphorylation of the loop regions. To explore this hypothesis, we used in vitro phosphorylation assays with a small panel of purified kinases and found that casein kinase 2 ( CK2) phosphorylates the Glu A1 and Glu A2 loop1 regions, but not Glu A3 or Glu A4. Interestingly, when we reduced the endogenous expression of CK2 using a specific short hairpin RNA against the regulatory subunit CK2β, we detected a reduction of Glu A1 surface expression, whereas Glu A2 was unchanged. Furthermore, we identified S579 of Glu A1 as a substrate of CK2, and the expression of Glu A1 phosphodeficient mutants in hippocampal neurons displayed reduced surface expression. Therefore, our study identifies CK2 as a regulator of Glu A1 surface expression by phosphorylating the intracellular loop1 region. [ABSTRACT FROM AUTHOR]

Published
2014
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