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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Autores principales: 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
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Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/82875625c72b4d9c8c7eaaf0131c13bc
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spelling oai:doaj.org-article:82875625c72b4d9c8c7eaaf0131c13bc2021-12-02T10:48:29ZThe Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation10.1038/s41467-020-19783-w2041-1723https://doaj.org/article/82875625c72b4d9c8c7eaaf0131c13bc2020-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19783-whttps://doaj.org/toc/2041-1723Hop, 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.Kaushik BhattacharyaLorenz WeidenauerTania Morán LuengoEllis C. PietersPablo C. EcheverríaLilia BernasconiDiana WiderYashar SadianMargreet B. KoopmanMatthieu VilleminChristoph BauerStefan G. D. RüdigerManfredo QuadroniDidier PicardNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-21 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
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
The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
description 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.
format article
author 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
author_facet 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
author_sort Kaushik Bhattacharya
title The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
title_short The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
title_full The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
title_fullStr The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
title_full_unstemmed The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
title_sort hsp70-hsp90 co-chaperone hop/stip1 shifts the proteostatic balance from folding towards degradation
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/82875625c72b4d9c8c7eaaf0131c13bc
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