Sis1 potentiates the stress response to protein aggregation and elevated temperature

Identifying factors that enable cells to induce a potent stress response to amyloid-like aggregation can provide further insight into the mechanism of stress regulation. Here, the authors express polyglutamine-expanded Huntingtin as a model disease protein in yeast cells and perform a genetic screen...

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Autores principales:	Courtney L. Klaips, Michael H. M. Gropp, Mark S. Hipp, F. Ulrich Hartl
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/bf06109c704f419bbd81a8c23509df78
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spelling	oai:doaj.org-article:bf06109c704f419bbd81a8c23509df782021-12-02T14:16:31ZSis1 potentiates the stress response to protein aggregation and elevated temperature10.1038/s41467-020-20000-x2041-1723https://doaj.org/article/bf06109c704f419bbd81a8c23509df782020-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20000-xhttps://doaj.org/toc/2041-1723Identifying factors that enable cells to induce a potent stress response to amyloid-like aggregation can provide further insight into the mechanism of stress regulation. Here, the authors express polyglutamine-expanded Huntingtin as a model disease protein in yeast cells and perform a genetic screen for chaperone factors that allow yeast cells to activate a potent stress response. They identify Sis1, an essential Hsp40 co-chaperone of Hsp70, as a critical sensor of proteotoxic stress and further show that both Sis1 and its mammalian homolog DnaJB6 regulate the magnitude of the cellular heat stress response, indicating that this mechanism is conserved.Courtney L. KlaipsMichael H. M. GroppMark S. HippF. Ulrich HartlNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Courtney L. Klaips Michael H. M. Gropp Mark S. Hipp F. Ulrich Hartl Sis1 potentiates the stress response to protein aggregation and elevated temperature
description	Identifying factors that enable cells to induce a potent stress response to amyloid-like aggregation can provide further insight into the mechanism of stress regulation. Here, the authors express polyglutamine-expanded Huntingtin as a model disease protein in yeast cells and perform a genetic screen for chaperone factors that allow yeast cells to activate a potent stress response. They identify Sis1, an essential Hsp40 co-chaperone of Hsp70, as a critical sensor of proteotoxic stress and further show that both Sis1 and its mammalian homolog DnaJB6 regulate the magnitude of the cellular heat stress response, indicating that this mechanism is conserved.
format	article
author	Courtney L. Klaips Michael H. M. Gropp Mark S. Hipp F. Ulrich Hartl
author_facet	Courtney L. Klaips Michael H. M. Gropp Mark S. Hipp F. Ulrich Hartl
author_sort	Courtney L. Klaips
title	Sis1 potentiates the stress response to protein aggregation and elevated temperature
title_short	Sis1 potentiates the stress response to protein aggregation and elevated temperature
title_full	Sis1 potentiates the stress response to protein aggregation and elevated temperature
title_fullStr	Sis1 potentiates the stress response to protein aggregation and elevated temperature
title_full_unstemmed	Sis1 potentiates the stress response to protein aggregation and elevated temperature
title_sort	sis1 potentiates the stress response to protein aggregation and elevated temperature
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/bf06109c704f419bbd81a8c23509df78
work_keys_str_mv	AT courtneylklaips sis1potentiatesthestressresponsetoproteinaggregationandelevatedtemperature AT michaelhmgropp sis1potentiatesthestressresponsetoproteinaggregationandelevatedtemperature AT markshipp sis1potentiatesthestressresponsetoproteinaggregationandelevatedtemperature AT fulrichhartl sis1potentiatesthestressresponsetoproteinaggregationandelevatedtemperature
_version_	1718391690083958784

Sis1 potentiates the stress response to protein aggregation and elevated temperature

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