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Your search keyword '"Koutelou, Evangelia"' showing total 18 results
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18 results on '"Koutelou, Evangelia"'

4. 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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8. 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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10. Histone H3K4 methylation regulates deactivation of the spindle assembly checkpoint through direct binding of Mad2

Author

Schibler, Andria, primary, Koutelou, Evangelia, additional, Tomida, Junya, additional, Wilson-Pham, Marenda, additional, Wang, Li, additional, Lu, Yue, additional, Cabrera, Alexa Parra, additional, Chosed, Renee J., additional, Li, Wenqian, additional, Li, Bing, additional, Shi, Xiaobing, additional, Wood, Richard D., additional, and Dent, Sharon Y.R., additional

Published
2016
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11. 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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15. Ubp8 and SAGA Regulate Snf1 AMP Kinase Activity

Author

Wilson, Marenda A., primary, Koutelou, Evangelia, additional, Hirsch, Calley, additional, Akdemir, Kadir, additional, Schibler, Andria, additional, Barton, Michelle Craig, additional, and Dent, Sharon Y. R., additional

Published
2011
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18. Poly(Q) Expansions in ATXN7 Affect Solubility but Not Activity of the SAGA Deubiquitinating Module.

Author

Xianjiang Lan, Koutelou, Evangelia, Schibler, Andria C., Yi Chun Chen, Grant, Patrick A., and Dent, Sharon Y. R.

Subjects
*POLYGLUTAMINE, *SPINOCEREBELLAR ataxia, *GENE expression, *BIOLOGICAL aggregation, *LABORATORY mice
Abstract

Spinocerebellar ataxia type 7 (SCA7) is a debilitating neurodegenerative disease caused by expansion of a polyglutamine [poly(Q)] tract in ATXN7, a subunit of the deubiquitinase (DUB) module (DUBm) in the SAGA complex. The effects of ATXN7- poly(Q) on DUB activity are not known. To address this important question, we reconstituted the DUBm in vitro with either wild-type ATXN7 or a pathogenic form, ATXN7-92Q NT, with 92 Q residues at the N terminus (NT). We found that both forms of ATXN7 greatly enhance DUB activity but that ATXN7-92Q NT is largely insoluble unless it is incorporated into the DUBm. Cooverexpression of DUBm components in human astrocytes also promoted the solubility of ATXN7-92Q, inhibiting its aggregation into nuclear inclusions that sequester DUBm components, leading to global increases in ubiquitinated H2B (H2Bub) levels. Global H2Bub levels were also increased in the cerebellums of mice in a SCA7 mouse model. Our findings indicate that although ATXN7 poly(Q) expansions do not change the enzymatic activity of the DUBm, they likely contribute to SCA7 by initiating aggregates that sequester the DUBm away from its substrates. [ABSTRACT FROM AUTHOR]

Published
2015
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