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

Bhattacharya, Kaushik; Weidenauer, Lorenz; Luengo, Tania Morán; Pieters, Ellis C.; Echeverria, Pablo; Bernasconi, Lilia; Wider, Diana; Sadian, Yashar; Koopman, Margreet B.; Villemin, Matthieu; Bauer, Christoph Ruediger; Rüdiger, Stefan G. D.; Quadroni, Manfredo; Picard, Didier

doi:10.1038/s41467-020-19783-w

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Title		The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
Authors		Bhattacharya, Kaushik Weidenauer, Lorenz Luengo, Tania Morán Pieters, Ellis C. Echeverria, Pablo Bernasconi, Lilia Wider, Diana Sadian, Yashar Koopman, Margreet B. Villemin, Matthieu Bauer, Christoph Ruediger Rüdiger, Stefan G. D. Quadroni, Manfredo Picard, Didier show all authors [1 - 14]
Published in		Nature communications. 2020, vol. 11, no. 5975
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 pro- teasome 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, com- pensates 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.
Identifiers		DOI: 10.1038/s41467-020-19783-w
Full text		Article (Published version) (13 MB) - Free access Other version: http://www.nature.com/articles/s41467-020-19783-w
Structures		Faculté des sciences / Section de biologie / Département de biologie cellulaire Faculté des sciences / Section de biologie / Département de génétique et évolution
Research group		Groupe Picard
Citation (ISO format)		BHATTACHARYA, Kaushik et al. The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation. In: Nature Communications, 2020, vol. 11, n° 5975. doi: 10.1038/s41467-020-19783-w https://archive-ouverte.unige.ch/unige:145478