PXD012774 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | The Hsp70/hsp90 Co-chaperone Hop/stip1 Shifts the Proteostatic Balance From Folding Towards Degradation |
Description | 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. 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. |
HostingRepository | PRIDE |
AnnounceDate | 2020-11-09 |
AnnouncementXML | Submission_2020-12-04_01:13:04.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Manfredo Quadroni |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | iodoacetamide derivatized residue |
Instrument | Orbitrap Fusion |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-02-18 23:51:50 | ID requested | |
1 | 2020-11-09 05:18:43 | announced | |
⏵ 2 | 2020-12-04 01:13:05 | announced | 2020-12-04: Updated publication reference for PubMed record(s): 33239621. |
Publication List
Bhattacharya K, Weidenauer L, Luengo TM, Pieters EC, Echeverr, í, a PC, Bernasconi L, Wider D, Sadian Y, Koopman MB, Villemin M, Bauer C, R, ü, diger 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 affiliation | Département de Biologie Cellulaire, Université de Genève |
contact email | didier.picard@unige.ch |
lab head | |
Manfredo Quadroni |
contact affiliation | University of Lausanne |
contact email | manfredo.quadroni@unil.ch |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD012774
- Label: PRIDE project
- Name: The Hsp70/hsp90 Co-chaperone Hop/stip1 Shifts the Proteostatic Balance From Folding Towards Degradation