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Ubiquitin-specific Peptidase 42 (USP42) Functions to Deubiquitylate Histones and Regulate Transcriptional Activity
Ubiquitin-specific peptidase 42 (USP42) is a deubiquitylating enzyme that can target p53 and contribute to the stabilization of p53 in response to stress. We now show that USP42 can also regulate transcription independently of p53. USP42 co-localized with RNA polymerase II (RNA Pol II) in nuclear fo...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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American Society for Biochemistry and Molecular Biology
2014
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4263885/ https://www.ncbi.nlm.nih.gov/pubmed/25336640 http://dx.doi.org/10.1074/jbc.M114.589267 |
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author | Hock, Andreas K. Vigneron, Arnaud M. Vousden, Karen H. |
author_facet | Hock, Andreas K. Vigneron, Arnaud M. Vousden, Karen H. |
author_sort | Hock, Andreas K. |
collection | PubMed |
description | Ubiquitin-specific peptidase 42 (USP42) is a deubiquitylating enzyme that can target p53 and contribute to the stabilization of p53 in response to stress. We now show that USP42 can also regulate transcription independently of p53. USP42 co-localized with RNA polymerase II (RNA Pol II) in nuclear foci, bound to histone H2B, and deubiquitylated H2B. Depletion of USP42 increased H2B ubiquitylation at a model promoter and decreased both basal and induced transcription from a number of promoters. These results are consistent with a role for USP42 in regulating transcription by deubiquitylating histones. |
format | Online Article Text |
id | pubmed-4263885 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-42638852014-12-16 Ubiquitin-specific Peptidase 42 (USP42) Functions to Deubiquitylate Histones and Regulate Transcriptional Activity Hock, Andreas K. Vigneron, Arnaud M. Vousden, Karen H. J Biol Chem Gene Regulation Ubiquitin-specific peptidase 42 (USP42) is a deubiquitylating enzyme that can target p53 and contribute to the stabilization of p53 in response to stress. We now show that USP42 can also regulate transcription independently of p53. USP42 co-localized with RNA polymerase II (RNA Pol II) in nuclear foci, bound to histone H2B, and deubiquitylated H2B. Depletion of USP42 increased H2B ubiquitylation at a model promoter and decreased both basal and induced transcription from a number of promoters. These results are consistent with a role for USP42 in regulating transcription by deubiquitylating histones. American Society for Biochemistry and Molecular Biology 2014-12-12 2014-10-21 /pmc/articles/PMC4263885/ /pubmed/25336640 http://dx.doi.org/10.1074/jbc.M114.589267 Text en © 2014 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version full access. Creative Commons Attribution Unported License (http://creativecommons.org/licenses/by/3.0/) applies to Author Choice Articles |
spellingShingle | Gene Regulation Hock, Andreas K. Vigneron, Arnaud M. Vousden, Karen H. Ubiquitin-specific Peptidase 42 (USP42) Functions to Deubiquitylate Histones and Regulate Transcriptional Activity |
title | Ubiquitin-specific Peptidase 42 (USP42) Functions to Deubiquitylate Histones and Regulate Transcriptional Activity |
title_full | Ubiquitin-specific Peptidase 42 (USP42) Functions to Deubiquitylate Histones and Regulate Transcriptional Activity |
title_fullStr | Ubiquitin-specific Peptidase 42 (USP42) Functions to Deubiquitylate Histones and Regulate Transcriptional Activity |
title_full_unstemmed | Ubiquitin-specific Peptidase 42 (USP42) Functions to Deubiquitylate Histones and Regulate Transcriptional Activity |
title_short | Ubiquitin-specific Peptidase 42 (USP42) Functions to Deubiquitylate Histones and Regulate Transcriptional Activity |
title_sort | ubiquitin-specific peptidase 42 (usp42) functions to deubiquitylate histones and regulate transcriptional activity |
topic | Gene Regulation |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4263885/ https://www.ncbi.nlm.nih.gov/pubmed/25336640 http://dx.doi.org/10.1074/jbc.M114.589267 |
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