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PXD012774 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleThe Hsp70/hsp90 Co-chaperone Hop/stip1 Shifts the Proteostatic Balance From Folding Towards Degradation
DescriptionHop/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. Similarly to budding yeast (ref), human cell lines 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 an alternate proteostatic equilibrium. Thus, Hop may be actionable for cells to shift the proteostatic balance between folding and degradation.
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterManfredo Quadroni
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListiodoacetamide derivatized residue
InstrumentOrbitrap Fusion
Dataset History
RevisionDatetimeStatusChangeLog Entry
02019-02-18 23:51:50ID requested
12020-11-09 05:18:43announced
22020-12-04 01:13:05announced2020-12-04: Updated publication reference for PubMed record(s): 33239621.
Publication List
Bhattacharya K, Weidenauer L, Luengo TM, Pieters EC, Echeverría PC, Bernasconi L, Wider D, Sadian Y, Koopman MB, Villemin M, Bauer C, Rüdiger SGD, Quadroni M, Picard D, The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation. Nat Commun, 11(1):5975(2020) [pubmed]
Keyword List
curator keyword: Biological
submitter keyword: Proteostasis, Hop, Proteasome, Molecular chaperone, Protein folding, Protein degradation, Hsp90, Hsp70, Protein quality control
Contact List
Didier Picard
contact affiliationDépartement de Biologie Cellulaire, Université de Genève
contact emaildidier.picard@unige.ch
lab head
Manfredo Quadroni
contact affiliationUniversity of Lausanne
contact emailmanfredo.quadroni@unil.ch
dataset submitter
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