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Sequential posttranslational modifications regulate PKC degradation
Cross-talk among different types of posttranslational modifications (PTMs) has emerged as an important regulatory mechanism for protein function. Here we elucidate a mechanism that controls PKCα stability via a sequential cascade of PTMs. We demonstrate that PKCα dephosphorylation decreases its sumo...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4713141/ https://www.ncbi.nlm.nih.gov/pubmed/26564794 http://dx.doi.org/10.1091/mbc.E15-09-0624 |
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author | Wang, Yan Wang, Yangbo Zhang, Huijun Gao, Yingwei Huang, Chao Zhou, Aiwu Zhou, Yi Li, Yong |
author_facet | Wang, Yan Wang, Yangbo Zhang, Huijun Gao, Yingwei Huang, Chao Zhou, Aiwu Zhou, Yi Li, Yong |
author_sort | Wang, Yan |
collection | PubMed |
description | Cross-talk among different types of posttranslational modifications (PTMs) has emerged as an important regulatory mechanism for protein function. Here we elucidate a mechanism that controls PKCα stability via a sequential cascade of PTMs. We demonstrate that PKCα dephosphorylation decreases its sumoylation, which in turn promotes its ubiquitination and ultimately enhances its degradation via the ubiquitin-proteasome pathway. These findings provide a molecular explanation for the activation-induced down-regulation of PKC proteins. |
format | Online Article Text |
id | pubmed-4713141 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-47131412016-03-30 Sequential posttranslational modifications regulate PKC degradation Wang, Yan Wang, Yangbo Zhang, Huijun Gao, Yingwei Huang, Chao Zhou, Aiwu Zhou, Yi Li, Yong Mol Biol Cell Articles Cross-talk among different types of posttranslational modifications (PTMs) has emerged as an important regulatory mechanism for protein function. Here we elucidate a mechanism that controls PKCα stability via a sequential cascade of PTMs. We demonstrate that PKCα dephosphorylation decreases its sumoylation, which in turn promotes its ubiquitination and ultimately enhances its degradation via the ubiquitin-proteasome pathway. These findings provide a molecular explanation for the activation-induced down-regulation of PKC proteins. The American Society for Cell Biology 2016-01-15 /pmc/articles/PMC4713141/ /pubmed/26564794 http://dx.doi.org/10.1091/mbc.E15-09-0624 Text en © 2016 Wang, Wang, Zhang, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Articles Wang, Yan Wang, Yangbo Zhang, Huijun Gao, Yingwei Huang, Chao Zhou, Aiwu Zhou, Yi Li, Yong Sequential posttranslational modifications regulate PKC degradation |
title | Sequential posttranslational modifications regulate PKC degradation |
title_full | Sequential posttranslational modifications regulate PKC degradation |
title_fullStr | Sequential posttranslational modifications regulate PKC degradation |
title_full_unstemmed | Sequential posttranslational modifications regulate PKC degradation |
title_short | Sequential posttranslational modifications regulate PKC degradation |
title_sort | sequential posttranslational modifications regulate pkc degradation |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4713141/ https://www.ncbi.nlm.nih.gov/pubmed/26564794 http://dx.doi.org/10.1091/mbc.E15-09-0624 |
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