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Posttranslational regulation of the GCN5 and PCAF acetyltransferases
General control nonderepressible 5 protein (Gcn5) and its homologs, including p300/CBP-associated factor (PCAF), are lysine acetyltransferases that modify both histone and non-histone proteins using acetyl coenzyme A as a donor substrate. While decades of studies have uncovered a vast network of cel...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Public Library of Science
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9477270/ https://www.ncbi.nlm.nih.gov/pubmed/36107838 http://dx.doi.org/10.1371/journal.pgen.1010352 |
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author | Ononye, Onyekachi E. Downey, Michael |
author_facet | Ononye, Onyekachi E. Downey, Michael |
author_sort | Ononye, Onyekachi E. |
collection | PubMed |
description | General control nonderepressible 5 protein (Gcn5) and its homologs, including p300/CBP-associated factor (PCAF), are lysine acetyltransferases that modify both histone and non-histone proteins using acetyl coenzyme A as a donor substrate. While decades of studies have uncovered a vast network of cellular processes impacted by these acetyltransferases, including gene transcription and metabolism, far less is known about how these enzymes are themselves regulated. In this review, we summarize the type and functions of posttranslational modifications proposed to control Gcn5 in both yeast and human cells. We further outline common themes, open questions, and strategies to guide future work. |
format | Online Article Text |
id | pubmed-9477270 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-94772702022-09-16 Posttranslational regulation of the GCN5 and PCAF acetyltransferases Ononye, Onyekachi E. Downey, Michael PLoS Genet Review General control nonderepressible 5 protein (Gcn5) and its homologs, including p300/CBP-associated factor (PCAF), are lysine acetyltransferases that modify both histone and non-histone proteins using acetyl coenzyme A as a donor substrate. While decades of studies have uncovered a vast network of cellular processes impacted by these acetyltransferases, including gene transcription and metabolism, far less is known about how these enzymes are themselves regulated. In this review, we summarize the type and functions of posttranslational modifications proposed to control Gcn5 in both yeast and human cells. We further outline common themes, open questions, and strategies to guide future work. Public Library of Science 2022-09-15 /pmc/articles/PMC9477270/ /pubmed/36107838 http://dx.doi.org/10.1371/journal.pgen.1010352 Text en © 2022 Ononye, Downey https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Review Ononye, Onyekachi E. Downey, Michael Posttranslational regulation of the GCN5 and PCAF acetyltransferases |
title | Posttranslational regulation of the GCN5 and PCAF acetyltransferases |
title_full | Posttranslational regulation of the GCN5 and PCAF acetyltransferases |
title_fullStr | Posttranslational regulation of the GCN5 and PCAF acetyltransferases |
title_full_unstemmed | Posttranslational regulation of the GCN5 and PCAF acetyltransferases |
title_short | Posttranslational regulation of the GCN5 and PCAF acetyltransferases |
title_sort | posttranslational regulation of the gcn5 and pcaf acetyltransferases |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9477270/ https://www.ncbi.nlm.nih.gov/pubmed/36107838 http://dx.doi.org/10.1371/journal.pgen.1010352 |
work_keys_str_mv | AT ononyeonyekachie posttranslationalregulationofthegcn5andpcafacetyltransferases AT downeymichael posttranslationalregulationofthegcn5andpcafacetyltransferases |