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

  • Bhattacharya K Département de Biologie Cellulaire, Université de Genève, Sciences III, 1211, Genève 4, Switzerland.
  • Weidenauer L Protein Analysis Facility, Center for Integrative Genomics, Université de Lausanne, 1015, Lausanne, Switzerland.
  • Luengo TM Cellular Protein Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, 3584, CH, Utrecht, The Netherlands.
  • Pieters EC Cellular Protein Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, 3584, CH, Utrecht, The Netherlands.
  • Echeverría PC Département de Biologie Cellulaire, Université de Genève, Sciences III, 1211, Genève 4, Switzerland.
  • Bernasconi L Département de Biologie Cellulaire, Université de Genève, Sciences III, 1211, Genève 4, Switzerland.
  • Wider D Département de Biologie Cellulaire, Université de Genève, Sciences III, 1211, Genève 4, Switzerland.
  • Sadian Y Bioimaging Center, Université de Genève, Sciences II, 1211, Genève 4, Switzerland.
  • Koopman MB Cellular Protein Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, 3584, CH, Utrecht, The Netherlands.
  • Villemin M Département de Biologie Cellulaire, Université de Genève, Sciences III, 1211, Genève 4, Switzerland.
  • Bauer C Bioimaging Center, Université de Genève, Sciences II, 1211, Genève 4, Switzerland.
  • Rüdiger SGD Cellular Protein Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, 3584, CH, Utrecht, The Netherlands.
  • Quadroni M Protein Analysis Facility, Center for Integrative Genomics, Université de Lausanne, 1015, Lausanne, Switzerland.
  • Picard D Département de Biologie Cellulaire, Université de Genève, Sciences III, 1211, Genève 4, Switzerland. didier.picard@unige.ch.
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  • 2020-11-26
Published in:
  • Nature communications. - 2020
General Biochemistry, Genetics and Molecular Biology
General Physics and Astronomy
General Chemistry
English 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.
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  • English
Open access status
gold
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https://sonar.ch/global/documents/46908
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