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Protein Methylation and Stress Granules: Posttranslational Remodeler or Innocent Bystander?

Stress granules contain a large number of post-translationally modified proteins, and studies have shown that these modifications serve as recruitment tags for specific proteins and even control the assembly and disassembly of the granules themselves. Work originating from our laboratory has focused...

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Detalles Bibliográficos
Autores principales: Xie, Wen, Denman, Robert B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: SAGE-Hindawi Access to Research 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3196864/
https://www.ncbi.nlm.nih.gov/pubmed/22091395
http://dx.doi.org/10.4061/2011/137459
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author Xie, Wen
Denman, Robert B.
author_facet Xie, Wen
Denman, Robert B.
author_sort Xie, Wen
collection PubMed
description Stress granules contain a large number of post-translationally modified proteins, and studies have shown that these modifications serve as recruitment tags for specific proteins and even control the assembly and disassembly of the granules themselves. Work originating from our laboratory has focused on the role protein methylation plays in stress granule composition and function. We have demonstrated that both asymmetrically and symmetrically dimethylated proteins are core constituents of stress granules, and we have endeavored to understand when and how this occurs. Here we seek to integrate this data into a framework consisting of the currently known post-translational modifications affecting stress granules to produce a model of stress granule dynamics that, in turn, may serve as a benchmark for understanding and predicting how post-translational modifications regulate other granule types.
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spelling pubmed-31968642011-11-16 Protein Methylation and Stress Granules: Posttranslational Remodeler or Innocent Bystander? Xie, Wen Denman, Robert B. Mol Biol Int Review Article Stress granules contain a large number of post-translationally modified proteins, and studies have shown that these modifications serve as recruitment tags for specific proteins and even control the assembly and disassembly of the granules themselves. Work originating from our laboratory has focused on the role protein methylation plays in stress granule composition and function. We have demonstrated that both asymmetrically and symmetrically dimethylated proteins are core constituents of stress granules, and we have endeavored to understand when and how this occurs. Here we seek to integrate this data into a framework consisting of the currently known post-translational modifications affecting stress granules to produce a model of stress granule dynamics that, in turn, may serve as a benchmark for understanding and predicting how post-translational modifications regulate other granule types. SAGE-Hindawi Access to Research 2011 2011-02-24 /pmc/articles/PMC3196864/ /pubmed/22091395 http://dx.doi.org/10.4061/2011/137459 Text en Copyright © 2011 W. Xie and R. B. Denman. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Xie, Wen
Denman, Robert B.
Protein Methylation and Stress Granules: Posttranslational Remodeler or Innocent Bystander?
title Protein Methylation and Stress Granules: Posttranslational Remodeler or Innocent Bystander?
title_full Protein Methylation and Stress Granules: Posttranslational Remodeler or Innocent Bystander?
title_fullStr Protein Methylation and Stress Granules: Posttranslational Remodeler or Innocent Bystander?
title_full_unstemmed Protein Methylation and Stress Granules: Posttranslational Remodeler or Innocent Bystander?
title_short Protein Methylation and Stress Granules: Posttranslational Remodeler or Innocent Bystander?
title_sort protein methylation and stress granules: posttranslational remodeler or innocent bystander?
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3196864/
https://www.ncbi.nlm.nih.gov/pubmed/22091395
http://dx.doi.org/10.4061/2011/137459
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