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

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

Hop, also known as Stip1 or Sti1, facilitates substrate transfer between the Hsp70 and Hsp90 molecular chaperones. Characterization of proteostasis-related pathways in STIP1 knock-out cell lines reveals that in eukaryotes Stip1 modulates the balance between protein folding and degradation.

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Bibliographic Details
Main Authors: 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, Didier Picard
Format: article
Language:EN
Published: Nature Portfolio 2020
Subjects:
Science
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Online Access:https://doaj.org/article/82875625c72b4d9c8c7eaaf0131c13bc
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Summary:Hop, also known as Stip1 or Sti1, facilitates substrate transfer between the Hsp70 and Hsp90 molecular chaperones. Characterization of proteostasis-related pathways in STIP1 knock-out cell lines reveals that in eukaryotes Stip1 modulates the balance between protein folding and degradation.

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