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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Nature Portfolio
2020
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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) |
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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 |
work_keys_str_mv |
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