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An Hsp90 co-chaperone links protein folding and degradation and is part of a conserved protein quality control

Eisele, Frederik and Eisele-Bürger, Anna Maria and Hao, Xinxin and Berglund, Lisa Larsson and Hoog, Johanna L. and Liu, Beidong and Nystrom, Thomas (2021). An Hsp90 co-chaperone links protein folding and degradation and is part of a conserved protein quality control. Cell Reports. 35 :13 , 109328
[Research article]

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Abstract

In this paper, we show that the essential Hsp90 co-chaperone Sgt1 is a member of a general protein quality control network that links folding and degradation through its participation in the degradation of misfolded proteins both in the cytosol and the endoplasmic reticulum (ER). Sgt1-dependent protein degradation acts in a parallel pathway to the ubiquitin ligase (E3) and ubiquitin chain elongase (E4), Hul5, and overproduction of Hul5 partly suppresses defects in cells with reduced Sgt1 activity. Upon proteostatic stress, Sgt1 accumu- lates transiently, in an Hsp90- and proteasome-dependent manner, with quality control sites (Q-bodies) of both yeast and human cells that co-localize with Vps13, a protein that creates organelle contact sites. Misfolding disease proteins, such as synphilin-1 involved in Parkinson's disease, are also sequestered to these compartments and require Sgt1 for their clearance.

Authors/Creators:Eisele, Frederik and Eisele-Bürger, Anna Maria and Hao, Xinxin and Berglund, Lisa Larsson and Hoog, Johanna L. and Liu, Beidong and Nystrom, Thomas
Title:An Hsp90 co-chaperone links protein folding and degradation and is part of a conserved protein quality control
Series Name/Journal:Cell Reports
Year of publishing :2021
Volume:35
Number:13
Article number:109328
Number of Pages:18
ISSN:2211-1247
Language:English
Publication Type:Research article
Article category:Scientific peer reviewed
Version:Published version
Copyright:Creative Commons: Attribution 4.0
Full Text Status:Public
Subjects:(A) Swedish standard research categories 2011 > 1 Natural sciences > 106 Biological Sciences (Medical to be 3 and Agricultural to be 4) > Cell Biology
URN:NBN:urn:nbn:se:slu:epsilon-p-114684
Permanent URL:
http://urn.kb.se/resolve?urn=urn:nbn:se:slu:epsilon-p-114684
Additional ID:
Type of IDID
DOI10.1016/j.celrep.2021.109328
Web of Science (WoS)000668072600020
ID Code:27146
Faculty:NJ - Fakulteten för naturresurser och jordbruksvetenskap
Department:(NL, NJ) > Department of Molecular Sciences
Deposited By: SLUpub Connector
Deposited On:18 Feb 2022 13:25
Metadata Last Modified:18 Feb 2022 13:31

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