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Article

A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins.

The Journal of cell biology - 2 Apr 2018

Grousl Tomas, Ungelenk Sophia, Miller Stephanie, Ho Chi-Ting, Khokhrina Maria, Mayer Matthias P, Bukau Bernd, Mogk Axel

Abstract excerpt

Chaperones with aggregase activity promote and organize the aggregation of misfolded proteins and their deposition at specific intracellular sites. This activity represents a novel cytoprotective strategy of protein quality control systems; however, little is known about its mechanism. In yeast, the small heat shock protein Hsp42 orchestrates the stress-induced sequestration of misfolded proteins into cytosolic...

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Identifiers

PMID: 29362223
DOI: 10.1083/jcb.201708116
PMCID: PMC5881502

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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