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Sgt1 interactome analysis under proteostatic stress and steady state conditions

ABSTRACT: Buildup of misfolded proteins are prevented by chaperone-assisted refolding and/or proteasome dependent degradation. The coordination of these two protein quality control (PQC) systems is not fully understood. We identified the essential Hsp90 co-chaperone Sgt1 as a new member of a general PQC linking folding and degradation. Upon proteostatic stress, e.g. heat shock, Sgt1 accumulates in an Hsp90- and proteasome dependent manner at an until now unknown spatial PQC compartment in both yeast and human cells. In order to find further components of this new PQC compartment we performed pull down experiments and a protein interaction analysis of cells expressing either GFP tagged Sgt1 (or GFP alone, as a negative control) that were either grown at 30Â°C or under heat shock conditions (42Â°C, 30 minutes).

INSTRUMENT(S): Q Exactive

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Frank Stein

LAB HEAD: Thomas Nystroem

PROVIDER: PXD016174 | Pride | 2021-07-02

REPOSITORIES: Pride

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

Eisele Frederik F Eisele-Bürger Anna Maria AM Hao Xinxin X Berglund Lisa Larsson LL Höög Johanna L JL Liu Beidong B Nyström Thomas T

Cell reports 20210601 13

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 activit ...[more]

PMID: 34192536

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