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207 results on '"Gergely, Fanni"'

4. A histone deacetylase 3 and mitochondrial complex I axis regulates toxic formaldehyde production

Author

Wit, Niek, primary, Gogola, Ewa, additional, West, James A., additional, Vornbäumen, Tristan, additional, Seear, Rachel V., additional, Bailey, Peter S. J., additional, Burgos-Barragan, Guillermo, additional, Wang, Meng, additional, Krawczyk, Patrycja, additional, Huberts, Daphne H. E. W., additional, Gergely, Fanni, additional, Matheson, Nicholas J., additional, Kaser, Arthur, additional, Nathan, James A., additional, and Patel, Ketan J., additional

Published
2023
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6. Myeloid cell interferon secretion restricts Zika flavivirus infection of developing and malignant human neural progenitor cells

Author

Bulstrode, Harry, primary, Girdler, Gemma C., additional, Gracia, Tannia, additional, Aivazidis, Alexander, additional, Moutsopoulos, Ilias, additional, Young, Adam M.H., additional, Hancock, John, additional, He, Xiaoling, additional, Ridley, Katherine, additional, Xu, Zhaoyang, additional, Stockley, John H., additional, Finlay, John, additional, Hallou, Clement, additional, Fajardo, Teodoro, additional, Fountain, Daniel M., additional, van Dongen, Stijn, additional, Joannides, Alexis, additional, Morris, Robert, additional, Mair, Richard, additional, Watts, Colin, additional, Santarius, Thomas, additional, Price, Stephen J., additional, Hutchinson, Peter J.A., additional, Hodson, Emma J., additional, Pollard, Steven M., additional, Mohorianu, Irina, additional, Barker, Roger A., additional, Sweeney, Trevor R., additional, Bayraktar, Omer, additional, Gergely, Fanni, additional, and Rowitch, David H., additional

Published
2022
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7. Centrosome function is critical during terminal erythroid differentiation

Author

Tátrai, Péter, Gergely, Fanni, Gergely, Fanni [0000-0002-2441-8095], and Apollo - University of Cambridge Repository

Subjects
Centrosome, General Immunology and Microbiology, General Neuroscience, Mitosis, Cell Cycle Proteins, Spindle Apparatus, Microtubules, General Biochemistry, Genetics and Molecular Biology, Mice, blood, mitotic spindle, hemic and lymphatic diseases, Chromosome Segregation, Animals, Anemia, Macrocytic, Molecular Biology, enucleation, erythropoiesis
Abstract

Red blood cells are produced by terminal erythroid differentiation, which involves the dramatic morphological transformation of erythroblasts into enucleated reticulocytes. Microtubules are important for enucleation, but it is not known if the centrosome, a key microtubule-organizing center, is required as well. Mice lacking the conserved centrosome component, CDK5RAP2, are likely to have defective erythroid differentiation because they develop macrocytic anemia. Here, we show that fetal liver-derived, CDK5RAP2-deficient erythroid progenitors generate fewer and larger reticulocytes, hence recapitulating features of macrocytic anemia. In erythroblasts, but not in embryonic fibroblasts, loss of CDK5RAP2 or pharmacological depletion of centrosomes leads to highly aberrant spindle morphologies. Consistent with such cells exiting mitosis without chromosome segregation, tetraploidy is frequent in late-stage erythroblasts, thereby giving rise to fewer but larger reticulocytes than normal. Our results define a critical role for CDK5RAP2 and centrosomes in spindle formation specifically during blood production. We propose that disruption of centrosome and spindle function could contribute to the emergence of macrocytic anemias, for instance, due to nutritional deficiency or exposure to chemotherapy.

Published
2022

11. The Myeloid Cell Secretome Regulates Zika Flavivirus Infection of Developing and Malignant Human Neural Progenitor Cells

Author

Bulstrode, Harry, primary, Girdler, Gemma C., additional, Gracia, Tannia, additional, Aivazidis, Alexander, additional, Moutsopoulos, Ilias, additional, Young, Adam MH, additional, Hancock, John, additional, He, X., additional, Ridley, Katherine, additional, Xu, Zhaoyang, additional, Stockley, John H., additional, Hallou, Clément, additional, Fajardo, Teodoro, additional, Fountain, Daniel M., additional, van Dongen, Stijn, additional, Joannides, Alexis, additional, Morris, Robert, additional, Mair, Richard, additional, Watts, Colin, additional, Santarius, Thomas, additional, Price, Stephen J., additional, Hutchinson, Peter, additional, Hodson, Emma J., additional, Pollard, Steven M., additional, Mohorianu, Irina, additional, Barker, Roger A., additional, Sweeney, Trevor R., additional, Bayraktar, Omer, additional, Gergely, Fanni, additional, and Rowitch, David, additional

Published
2022
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12. The Microglial Secretome Regulates Flavivirus Infection of Developing and Malignant Human Neural Stem Cells

Author

Bulstrode, Harry, primary, Girdler, Gemma C., additional, Gracia, Tannia, additional, Aivazidis, Alexander, additional, Moutsopoulos, Ilias, additional, Young, Adam MH, additional, He, X., additional, Ridley, Katherine, additional, Xu, Zhaoyang, additional, Stockley, John H., additional, Hallou, Clement, additional, Fajardo, Teodoro, additional, Fountain, Daniel M., additional, van Dongen, Stijn, additional, Joannides, Alexis, additional, Morris, Robert, additional, Mair, Richard, additional, Watts, Colin, additional, Santarius, Thomas, additional, Price, Stephen J., additional, Hutchinson, Peter, additional, Hodson, Emma J., additional, Pollard, Steven M., additional, Mohorianu, Irina, additional, Barker, Roger A., additional, Sweeney, Trevor R., additional, Bayraktar, Omer, additional, Gergely, Fanni, additional, and Rowitch, David, additional

Published
2022
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16. Centriolar satellites are acentriolar assemblies of centrosomal proteins

Author

Gergely, Fanni, Gergely, Fanni [0000-0002-2441-8095], and Apollo - University of Cambridge Repository

Subjects
centrosome, satellites, composition, proteome, centrioles
Abstract

Centrioles are core structural elements of both centrosomes and cilia. Although cytoplasmic granules called centriolar satellites have been observed around these structures, lack of a comprehensive inventory of satellite proteins impedes our understanding of their ancestry. To address this, we performed mass spectrometry (MS)-based proteome profiling of centriolar satellites obtained by affinity purification of their key constituent, PCM1, from sucrose gradient fractions. We defined an interactome consisting of 223 proteins, which showed striking enrichment in centrosome components. The proteome also contained new structural and regulatory factors with roles in ciliogenesis. Quantitative MS on whole-cell and centriolar satellite proteomes of acentriolar cells was performed to reveal dependencies of satellite composition on intact centrosomes. Although, most components remained associated with PCM1 in acentriolar cells, reduced cytoplasmic and satellite levels were observed for a subset of centrosomal proteins. These results demonstrate that centriolar satellites and centrosomes form independently but share a substantial fraction of their proteomes. Dynamic exchange of proteins between these organelles could facilitate their adaptation to changing cellular environments during development, stress response and tissue homeostasis.

Published
2019
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18. Centrosomal TACCtics

Author

Gergely, Fanni

Subjects
Cells -- Research, Centrosomes -- Analysis, Protein metabolism -- Research, Biological sciences
Published
2002

20. CCDC61/VFL3 Is a Paralog of SAS6 and Promotes Ciliary Functions

Author

Ochi, Takashi, primary, Quarantotti, Valentina, additional, Lin, Huawen, additional, Jullien, Jerome, additional, Rosa e Silva, Ivan, additional, Boselli, Francesco, additional, Barnabas, Deepak D., additional, Johnson, Christopher M., additional, McLaughlin, Stephen H., additional, Freund, Stefan M.V., additional, Blackford, Andrew N., additional, Kimata, Yuu, additional, Goldstein, Raymond E., additional, Jackson, Stephen P., additional, Blundell, Tom L., additional, Dutcher, Susan K., additional, Gergely, Fanni, additional, and van Breugel, Mark, additional

Published
2020
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22. Identifying the Zika Virus Target Cell in Malignant Glioma

Author

Girdler, Gemma, primary, Gracia, Tannia, additional, Fountain, Daniel, additional, Fajardo Jr, Ted, additional, Finlay, Jack, additional, Hallou, Clément, additional, Pollard, Steve, additional, Sweeney, Trevor, additional, Gergely, Fanni, additional, Rowitch, David, additional, and Bulstrode, Harry, additional

Published
2019
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23. Disease-Associated Mutations in CEP120 Destabilize the Protein and Impair Ciliogenesis

Author

Joseph, Nimesh, Al-Jassar, Caezar, Johnson, Christopher M, Andreeva, Antonina, Barnabas, Deepak D, Freund, Stefan MV, Gergely, Fanni, Van Breugel, Mark, Gergely, Fanni [0000-0002-2441-8095], and Apollo - University of Cambridge Repository

Subjects
Jeuene syndrome, Models, Molecular, JATD, Organogenesis, Cell Cycle Proteins, basal body, Article, Cell Line, Mice, Protein Domains, Joubert syndrome, CEP120, centriole, Animals, Amino Acid Sequence, lcsh:QH301-705.5, Zebrafish, Centrioles, Centrosome, Protein Stability, Cell Cycle, cilia, Temperature, ciliopathy, lcsh:Biology (General), Mutation
Abstract

Summary Ciliopathies are a group of genetic disorders caused by a failure to form functional cilia. Due to a lack of structural information, it is currently poorly understood how ciliopathic mutations affect protein functionality to give rise to the underlying disease. Using X-ray crystallography, we show that the ciliopathy-associated centriolar protein CEP120 contains three C2 domains. The point mutations V194A and A199P, which cause Joubert syndrome (JS) and Jeune asphyxiating thoracic dystrophy (JATD), respectively, both reduce the thermostability of the second C2 domain by targeting residues that point toward its hydrophobic core. Genome-engineered cells homozygous for these mutations have largely normal centriole numbers but show reduced CEP120 levels, compromised recruitment of distal centriole markers, and deficient cilia formation. Our results provide insight into the disease mechanism of two ciliopathic mutations in CEP120, identify putative binding partners of CEP120 C2B, and suggest a complex genotype-phenotype relation of the CEP120 ciliopathy alleles., Graphical Abstract, Highlights • The centriolar protein CEP120 contains three adjacent C2 domains (C2A–C2C) • Two ciliopathy-associated mutations in CEP120 C2B destabilize this domain in vitro • In cells, both mutations reduce cellular and centrosomal CEP120 levels • Both mutations impede distal centriole function and block cilia formation, Joseph et al. structurally and functionally characterize a conserved C2 domain of the centriolar protein CEP120, which harbors two distinct ciliopathy-associated mutations. Their results suggest that, by destabilizing the C2 domain, these mutations reduce cellular and centrosomal CEP120 levels, thereby causing abnormal distal centriolar function and defective ciliogenesis.

Published
2018

24. Mitotic spindle association of TACC3 requires Aurora-A-dependent stabilization of a cryptic α-helix

Author

Burgess, Selena G, Mukherjee, Manjeet, Sabir, Sarah, Joseph, Nimesh, Gutiérrez-Caballero, Cristina, Richards, Mark W, Huguenin-Dezot, Nicolas, Chin, Jason W, Kennedy, Eileen J, Pfuhl, Mark, Royle, Stephen J, Gergely, Fanni, Bayliss, Richard, Pfuhl, Mark [0000-0001-9592-6639], Royle, Stephen J [0000-0001-8927-6967], Gergely, Fanni [0000-0002-2441-8095], Bayliss, Richard [0000-0003-0604-2773], and Apollo - University of Cambridge Repository

Subjects
Protein Conformation, alpha-Helical, protein–protein interaction, phosphorylation, Humans, protein kinase, Spindle Apparatus, disorder–order transition, intrinsically disordered protein, Microtubule-Associated Proteins, Aurora Kinase A, Cell Line
Abstract

Aurora-A regulates the recruitment of TACC3 to the mitotic spindle through a phospho-dependent interaction with clathrin heavy chain (CHC). Here, we describe the structural basis of these interactions, mediated by three motifs in a disordered region of TACC3. A hydrophobic docking motif binds to a previously uncharacterized pocket on Aurora-A that is blocked in most kinases. Abrogation of the docking motif causes a delay in late mitosis, consistent with the cellular distribution of Aurora-A complexes. Phosphorylation of Ser558 engages a conformational switch in a second motif from a disordered state, needed to bind the kinase active site, into a helical conformation. The helix extends into a third, adjacent motif that is recognized by a helical-repeat region of CHC, not a recognized phospho-reader domain. This potentially widespread mechanism of phospho-recognition provides greater flexibility to tune the molecular details of the interaction than canonical recognition motifs that are dominated by phosphate binding.

Published
2018

26. Transcriptional silencing of long noncoding RNA GNG12-AS1 uncouples its transcriptional and product-related functions

Author

Stojic, Lovorka, Niemczyk, Malwina, Orjalo, Arturo, Ito, Yoko, Ruijter, Anna Elisabeth Maria, Uribe-Lewis, Santiago, Joseph, Nimesh, Weston, Stephen, Menon, Suraj, Odom, Duncan T., Rinn, John, Gergely, Fanni, Murrell, Adele, Odom, Duncan T [0000-0001-6201-5599], and Apollo - University of Cambridge Repository

Subjects
rho GTP-Binding Proteins, GTP-Binding Protein gamma Subunits, Science, Argonaute Proteins, Cell Cycle, Humans, Protein Isoforms, RNA Polymerase III, RNA Interference, RNA, Long Noncoding, Article, Oligonucleotide Array Sequence Analysis
Abstract

Long noncoding RNAs (lncRNAs) regulate gene expression via their RNA product or through transcriptional interference, yet a strategy to differentiate these two processes is lacking. To address this, we used multiple small interfering RNAs (siRNAs) to silence GNG12-AS1, a nuclear lncRNA transcribed in an antisense orientation to the tumour-suppressor DIRAS3. Here we show that while most siRNAs silence GNG12-AS1 post-transcriptionally, siRNA complementary to exon 1 of GNG12-AS1 suppresses its transcription by recruiting Argonaute 2 and inhibiting RNA polymerase II binding. Transcriptional, but not post-transcriptional, silencing of GNG12-AS1 causes concomitant upregulation of DIRAS3, indicating a function in transcriptional interference. This change in DIRAS3 expression is sufficient to impair cell cycle progression. In addition, the reduction in GNG12-AS1 transcripts alters MET signalling and cell migration, but these are independent of DIRAS3. Thus, differential siRNA targeting of a lncRNA allows dissection of the functions related to the process and products of its transcription., LncRNAs regulate gene expression via their RNA product and through transcriptional interference. Here, Stojic et al. uncouple these functions by using multiple siRNAs against GNG12-AS1 to show that this lncRNA has a product related role in MET signaling while its transcription modulates DIRAS3 expression.

Published
2016

31. Mitotic spindle association of TACC3 requires Aurora‐A‐dependent stabilization of a cryptic α‐helix

Author

Burgess, Selena G, primary, Mukherjee, Manjeet, additional, Sabir, Sarah, additional, Joseph, Nimesh, additional, Gutiérrez‐Caballero, Cristina, additional, Richards, Mark W, additional, Huguenin‐Dezot, Nicolas, additional, Chin, Jason W, additional, Kennedy, Eileen J, additional, Pfuhl, Mark, additional, Royle, Stephen J, additional, Gergely, Fanni, additional, and Bayliss, Richard, additional

Published
2018
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33. The ch-TOG/XMAP215 protein is essential for spindle pole organization in human somatic cells

Author

Gergely, Fanni, Draviam, Viji M., and Raff, Jordan W.

Subjects
Somatic cells -- Genetic aspects, Genetic research -- Analysis, Proteins -- Genetic aspects, Microtubules -- Genetic aspects, Biological sciences
Abstract

Research has been conducted on ch-TOG/XMAP215 proteins which bind to microtubules. The authors report that human somatic cells are more important for organizing spindle poles and less important for stabilizing spindle microtubules.

Published
2003

34. The TACC domain identifies a family of centrosomal proteins that can interact with microtubules

Author

Gergely, Fanni, Karlsson, Christina, Still, Ivan, Cowell, John, Kilmartin, John, and Raff, Jordan W.

Subjects
Centrosomes -- Physiological aspects, Microtubules -- Physiological aspects, Cell physiology -- Research, Mitosis -- Physiological aspects, Cancer -- Physiological aspects, Drosophila -- Physiological aspects, Tubulins -- Physiological aspects, Cell cycle -- Physiological aspects, Science and technology
Abstract

We recently showed that the Drosophila transforming acidic coiled-coil (D-TACC) protein is located in the centrosome, interacts with microtubules, and is required for mitosis in the Drosophila embryo. There are three known human TACC proteins that share a conserved, C-terminal, coiled-coil region with D-TACC. These proteins have all been implicated in cancer, but their normal functions are unknown. We show that all three human TACC proteins are concentrated at centrosomes, but with very different characteristics: TACC1 is weakly concentrated at centrosomes during mitosis; TACC2 is strongly concentrated at centrosomes throughout the cell cycle; and TACC3 is strongly concentrated in a more diffuse region around centrosomes during mitosis. When the C-terminal TACC domain is overexpressed in HeLa cells, it forms large polymers in the cytoplasm that can interact with both microtubules and tubulin. The full-length TACC proteins form similar polymers when overexpressed, but their interaction with microtubules and tubulin is regulated during the cell cycle. At least one of the human TACC proteins appears to increase the number and/or stability of centrosomal microtubules when overexpressed during mitosis. Thus, the TACC domain identifies a family of centrosomal proteins that can interact with microtubules. This may explain the link between the TACC genes and cancer. centrosome | cancer | mitosis

Published
2000

41. Abstract B96: Design, synthesis and biological evaluation of a novel allosteric inhibitor of HSET that damages cancer cells with supernumerary centrosomes.

Author

Watts, Ciorsdaidh A., primary, Richards, Frances M., additional, Bender, Andreas, additional, Bond, Peter J., additional, Korb, Oliver, additional, Kern, Oliver, additional, Riddick, Michelle, additional, Owen, Paul, additional, Myers, Rebecca M., additional, Raff, Jordan, additional, Gergely, Fanni, additional, Jodrell, Duncan I., additional, and Ley, Steven V., additional

Published
2013
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45. The Essential Role of Centrosomal NDE1 in Human Cerebral Cortex Neurogenesis

Author

Bakircioglu, Mehmet, primary, Carvalho, Ofélia P., additional, Khurshid, Maryam, additional, Cox, James J., additional, Tuysuz, Beyhan, additional, Barak, Tanyeri, additional, Yilmaz, Saliha, additional, Caglayan, Okay, additional, Dincer, Alp, additional, Nicholas, Adeline K., additional, Quarrell, Oliver, additional, Springell, Kelly, additional, Karbani, Gulshan, additional, Malik, Saghira, additional, Gannon, Caroline, additional, Sheridan, Eamonn, additional, Crosier, Moira, additional, Lisgo, Steve N., additional, Lindsay, Susan, additional, Bilguvar, Kaya, additional, Gergely, Fanni, additional, Gunel, Murat, additional, and Woods, C. Geoffrey, additional

Published
2011
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46. WDR62 is associated with the spindle pole and is mutated in human microcephaly

Author

Nicholas, Adeline K, primary, Khurshid, Maryam, additional, Désir, Julie, additional, Carvalho, Ofélia P, additional, Cox, James J, additional, Thornton, Gemma, additional, Kausar, Rizwana, additional, Ansar, Muhammad, additional, Ahmad, Wasim, additional, Verloes, Alain, additional, Passemard, Sandrine, additional, Misson, Jean-Paul, additional, Lindsay, Susan, additional, Gergely, Fanni, additional, Dobyns, William B, additional, Roberts, Emma, additional, Abramowicz, Marc, additional, and Woods, C Geoffrey, additional

Published
2010
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48. INPP5E mutations cause primary cilium signaling defects, ciliary instability and ciliopathies in human and mouse

Author

Jacoby, Monique, primary, Cox, James J, additional, Gayral, Stéphanie, additional, Hampshire, Daniel J, additional, Ayub, Mohammed, additional, Blockmans, Marianne, additional, Pernot, Eileen, additional, Kisseleva, Marina V, additional, Compère, Philippe, additional, Schiffmann, Serge N, additional, Gergely, Fanni, additional, Riley, John H, additional, Pérez-Morga, David, additional, Woods, C Geoffrey, additional, and Schurmans, Stéphane, additional

Published
2009
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