One domain fits all: Using disordered regions to sequester misfolded proteins

Small heat shock proteins (sHsps) are adenosine triphosphate–independent chaperones that protect cells from misfolded proteins. In this issue, Grousl et al. (2018. J. Cell Biol. https://doi.org/10.1083/jcb.201708116) show that the yeast sHsp Hsp42 uses a prion-like intrinsically disordered domain to...

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Detalles Bibliográficos
Autores principales: Boczek, Edgar E., Alberti, Simon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Rockefeller University Press 2018
Materias:
Commentaries
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5881514/
https://www.ncbi.nlm.nih.gov/pubmed/29523584
http://dx.doi.org/10.1083/jcb.201803015
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author Boczek, Edgar E.
Alberti, Simon
author_facet Boczek, Edgar E.
Alberti, Simon
author_sort Boczek, Edgar E.
collection PubMed
description Small heat shock proteins (sHsps) are adenosine triphosphate–independent chaperones that protect cells from misfolded proteins. In this issue, Grousl et al. (2018. J. Cell Biol. https://doi.org/10.1083/jcb.201708116) show that the yeast sHsp Hsp42 uses a prion-like intrinsically disordered domain to bind and sequester misfolded proteins in protein deposition sites.
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spelling pubmed-58815142018-10-02 One domain fits all: Using disordered regions to sequester misfolded proteins Boczek, Edgar E. Alberti, Simon J Cell Biol Commentaries Small heat shock proteins (sHsps) are adenosine triphosphate–independent chaperones that protect cells from misfolded proteins. In this issue, Grousl et al. (2018. J. Cell Biol. https://doi.org/10.1083/jcb.201708116) show that the yeast sHsp Hsp42 uses a prion-like intrinsically disordered domain to bind and sequester misfolded proteins in protein deposition sites. Rockefeller University Press 2018-04-02 /pmc/articles/PMC5881514/ /pubmed/29523584 http://dx.doi.org/10.1083/jcb.201803015 Text en © 2018 Boczek and Alberti http://www.rupress.org/terms/https://creativecommons.org/licenses/by-nc-sa/4.0/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 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Commentaries
Boczek, Edgar E.
Alberti, Simon
One domain fits all: Using disordered regions to sequester misfolded proteins
title One domain fits all: Using disordered regions to sequester misfolded proteins
title_full One domain fits all: Using disordered regions to sequester misfolded proteins
title_fullStr One domain fits all: Using disordered regions to sequester misfolded proteins
title_full_unstemmed One domain fits all: Using disordered regions to sequester misfolded proteins
title_short One domain fits all: Using disordered regions to sequester misfolded proteins
title_sort one domain fits all: using disordered regions to sequester misfolded proteins
topic Commentaries
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5881514/
https://www.ncbi.nlm.nih.gov/pubmed/29523584
http://dx.doi.org/10.1083/jcb.201803015
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