Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble

Small heat shock proteins (sHsps) form large spherical assemblies and their regulation is not well understood. Here, the authors provide insights into the mechanism of Hsp26 activation by characterising phospho-mimetic mutants of yeast Hsp26. They present cryo-EM structures of the wild-type Hsp26 40...

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Autores principales:	Moritz Mühlhofer, Carsten Peters, Thomas Kriehuber, Marina Kreuzeder, Pamina Kazman, Natalia Rodina, Bernd Reif, Martin Haslbeck, Sevil Weinkauf, Johannes Buchner
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/ba936da34061418da4605d6f906d2c8a
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spelling	oai:doaj.org-article:ba936da34061418da4605d6f906d2c8a2021-11-21T12:36:26ZPhosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble10.1038/s41467-021-27036-72041-1723https://doaj.org/article/ba936da34061418da4605d6f906d2c8a2021-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-27036-7https://doaj.org/toc/2041-1723Small heat shock proteins (sHsps) form large spherical assemblies and their regulation is not well understood. Here, the authors provide insights into the mechanism of Hsp26 activation by characterising phospho-mimetic mutants of yeast Hsp26. They present cryo-EM structures of the wild-type Hsp26 40mer and its phospho-mimetic mutants that reveal the location of the thermosensor in the oligomer, and the authors also show that the thermosensor domain is targeted by phosphorylation, which relieves the intrinsic inhibition of chaperone activity.Moritz MühlhoferCarsten PetersThomas KriehuberMarina KreuzederPamina KazmanNatalia RodinaBernd ReifMartin HaslbeckSevil WeinkaufJohannes BuchnerNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Moritz Mühlhofer Carsten Peters Thomas Kriehuber Marina Kreuzeder Pamina Kazman Natalia Rodina Bernd Reif Martin Haslbeck Sevil Weinkauf Johannes Buchner Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble
description	Small heat shock proteins (sHsps) form large spherical assemblies and their regulation is not well understood. Here, the authors provide insights into the mechanism of Hsp26 activation by characterising phospho-mimetic mutants of yeast Hsp26. They present cryo-EM structures of the wild-type Hsp26 40mer and its phospho-mimetic mutants that reveal the location of the thermosensor in the oligomer, and the authors also show that the thermosensor domain is targeted by phosphorylation, which relieves the intrinsic inhibition of chaperone activity.
format	article
author	Moritz Mühlhofer Carsten Peters Thomas Kriehuber Marina Kreuzeder Pamina Kazman Natalia Rodina Bernd Reif Martin Haslbeck Sevil Weinkauf Johannes Buchner
author_facet	Moritz Mühlhofer Carsten Peters Thomas Kriehuber Marina Kreuzeder Pamina Kazman Natalia Rodina Bernd Reif Martin Haslbeck Sevil Weinkauf Johannes Buchner
author_sort	Moritz Mühlhofer
title	Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble
title_short	Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble
title_full	Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble
title_fullStr	Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble
title_full_unstemmed	Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble
title_sort	phosphorylation activates the yeast small heat shock protein hsp26 by weakening domain contacts in the oligomer ensemble
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/ba936da34061418da4605d6f906d2c8a
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Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble

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