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

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

Publikováno v: Nature communications, vol. 11, no. 1, pp. 5975
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-21 (2020)
Nature Communications, Vol. 11, No 5975 (2020)

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 e

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

Autor: 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.; Science for Life, Utrecht University, 3584, CH, Utrecht, The Netherlands., Pieters EC; Cellular Protein Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, 3584, CH, Utrecht, The Netherlands.; Science for Life, Utrecht University, 3584, CH, Utrecht, The Netherlands., Echeverría PC; Département de Biologie Cellulaire, Université de Genève, Sciences III, 1211, Genève 4, Switzerland.; European Association for the Study of the Liver, 1203, Genève, 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.; Science for Life, 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.; Science for Life, 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.

Publikováno v: Nature communications [Nat Commun] 2020 Nov 25; Vol. 11 (1), pp. 5975. Date of Electronic Publication: 2020 Nov 25.