The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation

Kaushik Bhattacharya, Lorenz Weidenauer, Tania Morán Luengo, Ellis C. Pieters, Pablo C. Echeverría, Lilia Bernasconi, Diana Wider, Yashar Sadian, Margreet B. Koopman, Matthieu Villemin, Christoph Bauer, Stefan G. D. Rüdiger, Manfredo Quadroni and Didier Picard ()
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Kaushik Bhattacharya: Université de Genève
Lorenz Weidenauer: Université de Lausanne
Tania Morán Luengo: Utrecht University
Ellis C. Pieters: Utrecht University
Pablo C. Echeverría: Université de Genève
Lilia Bernasconi: Université de Genève
Diana Wider: Université de Genève
Yashar Sadian: Université de Genève
Margreet B. Koopman: Utrecht University
Matthieu Villemin: Université de Genève
Christoph Bauer: Université de Genève
Stefan G. D. Rüdiger: Utrecht University
Manfredo Quadroni: Université de Lausanne
Didier Picard: Université de Genève

Nature Communications, 2020, vol. 11, issue 1, 1-21

Abstract: Abstract Hop/Stip1/Sti1 is thought to be essential as a co-chaperone to facilitate substrate transfer between the Hsp70 and Hsp90 molecular chaperones. Despite this proposed key function for protein folding and maturation, it is not essential in a number of eukaryotes and bacteria lack an ortholog. We set out to identify and to characterize its eukaryote-specific function. Human cell lines and the budding yeast with deletions of the Hop/Sti1 gene display reduced proteasome activity due to inefficient capping of the core particle with regulatory particles. Unexpectedly, knock-out cells are more proficient at preventing protein aggregation and at promoting protein refolding. Without the restraint by Hop, a more efficient folding activity of the prokaryote-like Hsp70-Hsp90 complex, which can also be demonstrated in vitro, compensates for the proteasomal defect and ensures the proteostatic equilibrium. Thus, cells may act on the level and/or activity of Hop to shift the proteostatic balance between folding and degradation.

Date: 2020
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DOI: 10.1038/s41467-020-19783-w

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