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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...

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Detalles Bibliográficos
Autores principales: Wang, Yan, Wang, Yangbo, Zhang, Huijun, Gao, Yingwei, Huang, Chao, Zhou, Aiwu, Zhou, Yi, Li, Yong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2016
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.
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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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