Chaperone-facilitated aggregation of thermo-sensitive proteins shields them from degradation during heat stress

Mostra el registre complet Registre parcial de l'ítem

• dc.contributor.author Cabrera, Margarita
• dc.contributor.author Boronat i Llop, Susanna, 1965-
• dc.contributor.author Marte, Luis, 1990-
• dc.contributor.author Vega, Montserrat
• dc.contributor.author Pérez, Pilar
• dc.contributor.author Ayté del Olmo, José
• dc.contributor.author Hidalgo Hernando, Elena
• dc.date.accessioned 2020-03-11T08:34:11Z
• dc.date.available 2020-03-11T08:34:11Z
• dc.date.issued 2020
• dc.description.abstract Cells have developed protein quality-control strategies to manage the accumulation of misfolded substrates during heat stress. Using a soluble reporter of misfolding in fission yeast, Rho1.C17R-GFP, we demonstrate that upon mild heat shock, the reporter collapses in protein aggregate centers (PACs). They contain and/or require several chaperones, such as Hsp104, Hsp16, and the Hsp40/70 couple Mas5/Ssa2. Stress granules do not assemble at mild temperatures and, therefore, are not required for PAC formation; on the contrary, PACs may serve as nucleation centers for the assembly of stress granules. In contrast to the general belief, the dominant fate of these PACs is not degradation, and the aggregated reporter can be disassembled by chaperones and recovers native structure and activity. Using mass spectrometry, we show that thermo-unstable endogenous proteins form PACs as well. In conclusion, formation of PACs during heat shock is a chaperone-mediated adaptation strategy.
• dc.description.sponsorship This work is supported by the Ministerio de Ciencia, Innovación y Universidades, PLAN E, and FEDER (Spain) (PGC2018-093920-B-I00 to E.H. and BFU2016-75116-P to M.C.). The Oxidative Stress and Cell Cycle group is also supported by Generalitat de Catalunya (Spain) (2017-SGR-539) and by Unidad de Excelencia María de Maeztu from MINECO (Spain) (MDM-2014-0370). M.C. is funded by the Ramon y Cajal program (MINECO-RYC2013-12858). E.H. is a recipient of an ICREA Academia Award (Generalitat de Catalunya, Spain).
• dc.format.mimetype application/pdf
• dc.identifier.citation Cabrera M, Boronat S, Marte L, Vega M, Pérez P, Ayté J, Hidalgo E. Chaperone-facilitated aggregation of thermo-sensitive proteins shields them from degradation during heat stress. Cell Rep. 2020; 30(7):2430-43.e4. DOI: 10.1016/j.celrep.2020.01.077
• dc.identifier.doi http://dx.doi.org/10.1016/j.celrep.2020.01.077
• dc.identifier.issn 2211-1247
• dc.identifier.uri http://hdl.handle.net/10230/43854
• dc.language.iso eng
• dc.publisher Elsevier
• dc.relation.ispartof Cell Rep. 2020; 30(7):2430-43.e4
• dc.relation.projectID info:eu-repo/grantAgreement/ES/1PE/BFU2016-75116-P
• dc.rights © 2020 The Author(s).This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/)
• dc.rights.accessRights info:eu-repo/semantics/openAccess
• dc.rights.uri http://creativecommons.org/licenses/by-nc-nd/4.0/
• dc.subject.keyword Hsp104
• dc.subject.keyword J-protein
• dc.subject.keyword Mas5
• dc.subject.keyword PAC
• dc.subject.keyword PQC
• dc.subject.keyword UPS
• dc.subject.keyword Heat stress
• dc.subject.keyword Protein aggregates
• dc.subject.keyword Protein refolding
• dc.subject.keyword Stress granules
• dc.title Chaperone-facilitated aggregation of thermo-sensitive proteins shields them from degradation during heat stress
• dc.type info:eu-repo/semantics/article
• dc.type.version info:eu-repo/semantics/publishedVersion