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Your search keyword '"Atanassov, Boyko S."' showing total 27 results
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27 results on '"Atanassov, Boyko S."'

1. USP27X variants underlying X-linked intellectual disability disrupt protein function via distinct mechanisms

Author

Genetica Klinische Genetica, Koch, Intisar, Slovik, Maya, Zhang, Yuling, Liu, Bingyu, Rennie, Martin, Konz, Emily, Cogne, Benjamin, Daana, Muhannad, Davids, Laura, Diets, Illja J, Gold, Nina B, Holtz, Alexander M, Isidor, Bertrand, Mor-Shaked, Hagar, Neira Fresneda, Juanita, Niederhoffer, Karen Y, Nizon, Mathilde, Pfundt, Rolph, Simon, Meh, Stegmann, Apa, Guillen Sacoto, Maria J, Wevers, Marijke, Barakat, Tahsin Stefan, Yanovsky-Dagan, Shira, Atanassov, Boyko S, Toth, Rachel, Gao, Chengjiang, Bustos, Francisco, Harel, Tamar, Genetica Klinische Genetica, Koch, Intisar, Slovik, Maya, Zhang, Yuling, Liu, Bingyu, Rennie, Martin, Konz, Emily, Cogne, Benjamin, Daana, Muhannad, Davids, Laura, Diets, Illja J, Gold, Nina B, Holtz, Alexander M, Isidor, Bertrand, Mor-Shaked, Hagar, Neira Fresneda, Juanita, Niederhoffer, Karen Y, Nizon, Mathilde, Pfundt, Rolph, Simon, Meh, Stegmann, Apa, Guillen Sacoto, Maria J, Wevers, Marijke, Barakat, Tahsin Stefan, Yanovsky-Dagan, Shira, Atanassov, Boyko S, Toth, Rachel, Gao, Chengjiang, Bustos, Francisco, and Harel, Tamar

Published
2024

2. USP27X variants underlying X-linked intellectual disability disrupt protein function via distinct mechanisms

Author

Koch, Intisar, Slovik, Maya, Zhang, Yuling, Liu, Bingyu, Rennie, Martin, Konz, Emily, Cogne, Benjamin, Daana, Muhannad, Davids, Laura, Diets, Illja J., Gold, Nina B., Holtz, Alexander M., Isidor, Bertrand, Mor-Shaked, Hagar, Neira Fresneda, Juanita, Niederhoffer, Karen Y., Nizon, Mathilde, Pfundt, Rolph, Simon, Meh, Stegmann, Apa, Guillen Sacoto, Maria J., Wevers, Marijke, Barakat, Tahsin Stefan, Yanovsky-Dagan, Shira, Atanassov, Boyko S., Toth, Rachel, Gao, Chengjiang, Bustos, Francisco, Harel, Tamar, Koch, Intisar, Slovik, Maya, Zhang, Yuling, Liu, Bingyu, Rennie, Martin, Konz, Emily, Cogne, Benjamin, Daana, Muhannad, Davids, Laura, Diets, Illja J., Gold, Nina B., Holtz, Alexander M., Isidor, Bertrand, Mor-Shaked, Hagar, Neira Fresneda, Juanita, Niederhoffer, Karen Y., Nizon, Mathilde, Pfundt, Rolph, Simon, Meh, Stegmann, Apa, Guillen Sacoto, Maria J., Wevers, Marijke, Barakat, Tahsin Stefan, Yanovsky-Dagan, Shira, Atanassov, Boyko S., Toth, Rachel, Gao, Chengjiang, Bustos, Francisco, and Harel, Tamar

Abstract

Neurodevelopmental disorders with intellectual disability (ND/ID) are a heterogeneous group of diseases driving lifelong deficits in cognition and behavior with no definitive cure. X-linked intellectual disability disorder 105 (XLID105, #300984; OMIM) is a ND/ID driven by hemizygous variants in the USP27X gene encoding a protein deubiquitylase with a role in cell proliferation and neural development. Currently, only four genetically diagnosed individuals from two unrelated families have been described with limited clinical data. Furthermore, the mechanisms underlying the disorder are unknown. Here, we report 10 new XLID105 individuals from nine families and determine the impact of gene variants on USP27X protein function. Using a combination of clinical genetics, bioinformatics, biochemical, and cell biology approaches, we determined that XLID105 variants alter USP27X protein biology via distinct mechanisms including changes in developmentally relevant protein-protein interactions and deubiquitylating activity. Our data better define the phenotypic spectrum of XLID105 and suggest that XLID105 is driven by USP27X functional disruption. Understanding the pathogenic mechanisms of XLID105 variants will provide molecular insight into USP27X biology and may create the potential for therapy development.

Published
2024

3. USP27Xvariants underlying X-linked intellectual disability disrupt protein function via distinct mechanisms

Author

Koch, Intisar, primary, Slovik, Maya, additional, Zhang, Yuling, additional, Liu, Bingyu, additional, Rennie, Martin, additional, Konz, Emily, additional, Cogne, Benjamin, additional, Daana, Muhannad, additional, Davids, Laura, additional, Diets, Illja J, additional, Gold, Nina B, additional, Holtz, Alexander M, additional, Isidor, Bertrand, additional, Mor-Shaked, Hagar, additional, Neira Fresneda, Juanita, additional, Niederhoffer, Karen Y, additional, Nizon, Mathilde, additional, Pfundt, Rolph, additional, Simon, MEH, additional, Stegmann, APA, additional, Guillen Sacoto, Maria J, additional, Wevers, Marijke, additional, Barakat, Tahsin Stefan, additional, Yanovsky-Dagan, Shira, additional, Atanassov, Boyko S, additional, Toth, Rachel, additional, Gao, Chengjiang, additional, Bustos, Francisco, additional, and Harel, Tamar, additional

Published
2024
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11. Usp22 Overexpression Leads to Aberrant Signal Transduction of Cancer-Related Pathways but Is Not Sufficient to Drive Tumor Formation in Mice

Author

Kuang, Xianghong, primary, McAndrew, Michael J., additional, Mustachio, Lisa Maria, additional, Chen, Ying-Jiun C., additional, Atanassov, Boyko S., additional, Lin, Kevin, additional, Lu, Yue, additional, Shen, Jianjun, additional, Salinger, Andrew, additional, Macatee, Timothy, additional, Dent, Sharon Y. R., additional, and Koutelou, Evangelia, additional

Published
2021
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16. Usp22 controls multiple signaling pathways that are essential for vasculature formation in the mouse placenta

Author

Koutelou, Evangelia, primary, Wang, Li, additional, Schibler, Andria, additional, Chao, Hsueh-Ping, additional, Kuang, Xianghong, additional, Lin, Kevin, additional, Lu, Yue, additional, Shen, Jianjun, additional, Jeter, Collene R., additional, Salinger, Andrew, additional, Wilson, Marenda, additional, Chen, Yi Chun, additional, Atanassov, Boyko S., additional, Tang, Dean G., additional, and Dent, Sharon YR, additional

Published
2019
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17. TGFβ-Activated USP27X Deubiquitinase Regulates Cell Migration and Chemoresistance via Stabilization of Snail1

Author

Lambies, Guillem, primary, Miceli, Martina, additional, Martínez-Guillamon, Catalina, additional, Olivera-Salguero, Rubén, additional, Peña, Raúl, additional, Frías, Carolina-Paola, additional, Calderón, Irene, additional, Atanassov, Boyko S., additional, Dent, Sharon Y. R., additional, Arribas, Joaquín, additional, García de Herreros, Antonio, additional, and Díaz, Víctor M., additional

Published
2019
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20. ATXN7L3 and ENY2 Coordinate Activity of Multiple H2B Deubiquitinases Important for Cellular Proliferation and Tumor Growth

Author

Atanassov, Boyko S., primary, Mohan, Ryan D., additional, Lan, Xianjiang, additional, Kuang, Xianghong, additional, Lu, Yue, additional, Lin, Kevin, additional, McIvor, Elizabeth, additional, Li, Wenqian, additional, Zhang, Ying, additional, Florens, Laurence, additional, Byrum, Stephanie D., additional, Mackintosh, Samuel G., additional, Calhoun-Davis, Tammy, additional, Koutelou, Evangelia, additional, Wang, Li, additional, Tang, Dean G., additional, Tackett, Alan J., additional, Washburn, Michael P., additional, Workman, Jerry L., additional, and Dent, Sharon Y.R., additional

Published
2016
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21. Cytoplasmic ATXN7L3B Interferes with Nuclear Functions of the SAGA Deubiquitinase Module.

Author

Wenqian Li, Atanassov, Boyko S., Xianjiang Lan, Mohan, Ryan D., Swanson, Selene K., Farria, Aimee T., Florens, Laurence, Washburn, Michael P., Workman, Jerry L., and Dent, Sharon Y. R.

Subjects
*HISTONE deacetylase, *GENETICS of breast cancer, *GENE expression, *GENE targeting, *CANCER cells
Abstract

The SAGA complex contains two enzymatic modules, which house histone acetyltransferase (HAT) and deubiquitinase (DUB) activities. USP22 is the catalytic subunit of the DUB module, but two adaptor proteins, ATXN7L3 and ENY2, are necessary for DUB activity toward histone H2Bub1 and other substrates. ATXN7L3B shares 74% identity with the N-terminal region of ATXN7L3, but the functions of ATXN7L3B are not known. Here we report that ATXN7L3B interacts with ENY2 but not other SAGA components. Even though ATXN7L3B localizes in the cytoplasm, ATXN7L3B overexpression increases H2Bub1 levels, while overexpression of ATXN7L3 decreases H2Bub1 levels. In vitro, ATXN7L3B competes with ATXN7L3 to bind ENY2, and in vivo, knockdown of ATXN7L3B leads to concomitant loss of ENY2. Unlike the ATXN7L3 DUB complex, a USP22-ATXN7L3BENY2 complex cannot deubiquitinate H2Bub1 efficiently in vitro. Moreover, ATXN7L3B knockdown inhibits migration of breast cancer cells in vitro and limits expression of ER target genes. Collectively, our studies suggest that ATXN7L3B regulates H2Bub1 levels and SAGA DUB activity through competition for ENY2 binding. [ABSTRACT FROM AUTHOR]

Published
2016
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26. USP27X variants underlying X-linked intellectual disability disrupt protein function via distinct mechanisms.

Author

Koch I, Slovik M, Zhang Y, Liu B, Rennie M, Konz E, Cogne B, Daana M, Davids L, Diets IJ, Gold NB, Holtz AM, Isidor B, Mor-Shaked H, Neira Fresneda J, Niederhoffer KY, Nizon M, Pfundt R, Simon M, Stegmann A, Guillen Sacoto MJ, Wevers M, Barakat TS, Yanovsky-Dagan S, Atanassov BS, Toth R, Gao C, Bustos F, and Harel T

Subjects
Humans, Cell Proliferation, Computational Biology, Neurogenesis, Intellectual Disability genetics, Mental Retardation, X-Linked genetics
Abstract

Neurodevelopmental disorders with intellectual disability (ND/ID) are a heterogeneous group of diseases driving lifelong deficits in cognition and behavior with no definitive cure. X-linked intellectual disability disorder 105 (XLID105, #300984; OMIM) is a ND/ID driven by hemizygous variants in the USP27X gene encoding a protein deubiquitylase with a role in cell proliferation and neural development. Currently, only four genetically diagnosed individuals from two unrelated families have been described with limited clinical data. Furthermore, the mechanisms underlying the disorder are unknown. Here, we report 10 new XLID105 individuals from nine families and determine the impact of gene variants on USP27X protein function. Using a combination of clinical genetics, bioinformatics, biochemical, and cell biology approaches, we determined that XLID105 variants alter USP27X protein biology via distinct mechanisms including changes in developmentally relevant protein-protein interactions and deubiquitylating activity. Our data better define the phenotypic spectrum of XLID105 and suggest that XLID105 is driven by USP27X functional disruption. Understanding the pathogenic mechanisms of XLID105 variants will provide molecular insight into USP27X biology and may create the potential for therapy development., (© 2024 Koch et al.)

Published
2024
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27. Homozygous germ line mutation in exon 27 of murine Brca2 disrupts the Fancd2-Brca2 pathway in the homologous recombination-mediated DNA interstrand cross-links' repair but does not affect meiosis.

Author

Atanassov BS, Barrett JC, and Davis BJ

Subjects
Animals, BRCA2 Protein chemistry, Blotting, Western, Cell Nucleus metabolism, Cells, Cultured, Comet Assay, Embryo, Mammalian, Exons, Female, Fibroblasts drug effects, Fibroblasts radiation effects, Flow Cytometry, Fluorescent Antibody Technique, Indirect, Histones metabolism, Kinetics, Mice, Mitomycin pharmacology, Rad51 Recombinase metabolism, Radiation, Ionizing, BRCA2 Protein metabolism, DNA Repair, Fanconi Anemia Complementation Group D2 Protein metabolism, Germ-Line Mutation, Meiosis, Recombination, Genetic
Abstract

The role of the region encoded by exon 27 of the Brca2 gene in DNA repair was studied in cells and tissues from Brca2Delta27/Delta27 mice. The COOH-terminal truncated Brca2 localized to the nucleus in primary mouse embryo fibroblasts from Brca2Delta27/Delta27 mice. Fluorescence-activated cell sorting (FACS) analysis demonstrated that these fibroblasts were hypersensitive to mitomycin C-induced cross-links, but not to double-strand breaks (DSBs) induced by irradiation. The gammaH2AX appearance kinetics and comet assay showed that DSBs were repaired through non-homologous end joining pathways, while interstrand cross-links were not repaired due to deficient homologous recombination pathways. Immunoprecipitation experiments showed that Fancd2 did not coprecipitate with the mutated Brca2. There were also no detectable Rad51-positive foci formed in these cells after damage. On the other hand, we did not find any difference during gametogenesis in mice harboring exon 27 truncating mutation of the Brca2 gene and control mice, and in both cases, Rad51 localized to the recombination foci. Our results suggest that exon 27 of murine Brca2 is crucial for the interaction of Brca2 and Fancd2 in Rad51-mediated recombination in response to DNA damage, but that this interaction is not taking place in the homologous recombination during meiosis., (Published 2005 Wiley-Liss, Inc.)

Published
2005
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