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Article

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

Cell reports - 29 Jun 2021

Eisele Frederik, Eisele-Bürger Anna Maria, Hao Xinxin, Berglund Lisa Larsson, Höög Johanna L, Liu Beidong, Nyström Thomas

Abstract excerpt

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...

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Identifiers

PMID: 34192536
DOI: 10.1016/j.celrep.2021.109328

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