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Research article - Peer-reviewed, 2021

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

Eisele, Frederik; Eisele-Burger, Anna Maria; Hao, Xinxin; Berglund, Lisa Larsson; Hoog, Johanna L.; Liu, Beidong; Nystrom, Thomas


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.

Published in

Cell Reports
2021, volume: 35, number: 13, article number: 109328

Authors' information

Eisele, Frederik
University of Gothenburg
Eisele-Bürger, Anna Maria
Swedish University of Agricultural Sciences, Department of Molecular Sciences
Eisele-Bürger, Anna Maria
University of Gothenburg
Hao, Xinxin
University of Gothenburg
Berglund, Lisa Larsson
University of Gothenburg
Hoog, Johanna L.
University of Gothenburg
Liu, Beidong
University of Gothenburg
Nystrom, Thomas
University of Gothenburg

UKÄ Subject classification

Cell Biology

Publication Identifiers


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