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Mechanistic insights into mammalian stress granule dynamics

The accumulation of stalled translation preinitiation complexes (PICs) mediates the condensation of stress granules (SGs). Interactions between prion-related domains and intrinsically disordered protein regions found in SG-nucleating proteins promote the condensation of ribonucleoproteins into SGs....

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Detalles Bibliográficos
Autores principales: Panas, Marc D., Ivanov, Pavel, Anderson, Paul
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5100297/
https://www.ncbi.nlm.nih.gov/pubmed/27821493
http://dx.doi.org/10.1083/jcb.201609081
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author Panas, Marc D.
Ivanov, Pavel
Anderson, Paul
author_facet Panas, Marc D.
Ivanov, Pavel
Anderson, Paul
author_sort Panas, Marc D.
collection PubMed
description The accumulation of stalled translation preinitiation complexes (PICs) mediates the condensation of stress granules (SGs). Interactions between prion-related domains and intrinsically disordered protein regions found in SG-nucleating proteins promote the condensation of ribonucleoproteins into SGs. We propose that PIC components, especially 40S ribosomes and mRNA, recruit nucleators that trigger SG condensation. With resolution of stress, translation reinitiation reverses this process and SGs disassemble. By cooperatively modulating the assembly and disassembly of SGs, ribonucleoprotein condensation can influence the survival and recovery of cells exposed to unfavorable environmental conditions.
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spelling pubmed-51002972017-05-07 Mechanistic insights into mammalian stress granule dynamics Panas, Marc D. Ivanov, Pavel Anderson, Paul J Cell Biol Reviews The accumulation of stalled translation preinitiation complexes (PICs) mediates the condensation of stress granules (SGs). Interactions between prion-related domains and intrinsically disordered protein regions found in SG-nucleating proteins promote the condensation of ribonucleoproteins into SGs. We propose that PIC components, especially 40S ribosomes and mRNA, recruit nucleators that trigger SG condensation. With resolution of stress, translation reinitiation reverses this process and SGs disassemble. By cooperatively modulating the assembly and disassembly of SGs, ribonucleoprotein condensation can influence the survival and recovery of cells exposed to unfavorable environmental conditions. The Rockefeller University Press 2016-11-07 /pmc/articles/PMC5100297/ /pubmed/27821493 http://dx.doi.org/10.1083/jcb.201609081 Text en © 2016 Panas et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Reviews
Panas, Marc D.
Ivanov, Pavel
Anderson, Paul
Mechanistic insights into mammalian stress granule dynamics
title Mechanistic insights into mammalian stress granule dynamics
title_full Mechanistic insights into mammalian stress granule dynamics
title_fullStr Mechanistic insights into mammalian stress granule dynamics
title_full_unstemmed Mechanistic insights into mammalian stress granule dynamics
title_short Mechanistic insights into mammalian stress granule dynamics
title_sort mechanistic insights into mammalian stress granule dynamics
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5100297/
https://www.ncbi.nlm.nih.gov/pubmed/27821493
http://dx.doi.org/10.1083/jcb.201609081
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