PXD001214 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Rsp5/Nedd4 is the major ubiquitin ligase that targets cytosolic misfolded proteins upon heat-stress |
Description | The heat-shock response is a complex cellular program that induces major changes in protein translation, folding and degradation to alleviate toxicity caused by protein misfolding. While heat-shock has been widely used to study proteostasis, it remained unclear how misfolded proteins are targeted for proteolysis in these conditions. We found that Rsp5 and its mammalian homologue Nedd4 are the main E3-ligases responsible for the increased ubiquitination induced by heat-stress. We determined that Rsp5 ubiquitinates cytosolic misfolded proteins upon heat-shock for proteasome degradation. We found that ubiquitination of heat-induced substrates requires the Hsp40 co-chaperone Ydj1 that is further associated with Rsp5 upon heat-shock. Additionally, ubiquitination is also promoted by PY Rsp5-binding motifs found primarily in the structured regions of stress-induced substrates, which can act as heat-induced degrons. Our results support a bipartite recognition mechanism combining direct and chaperone-dependent ubiquitination of misfolded cytosolic proteins by Rsp5. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_04:03:50.663.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Neng Fang |
SpeciesList | scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932; |
ModificationList | carbamoylated residue; 6x(13)C; ubiquitination signature dipeptidyl lysine; phosphorylated residue; acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue; IMID d4 |
Instrument | LTQ Orbitrap Velos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2014-08-08 03:26:16 | ID requested | |
1 | 2016-07-06 06:04:30 | announced | |
⏵ 2 | 2024-10-22 04:03:56 | announced | 2024-10-22: Updated project metadata. |
Publication List
Fang NN, Chan GT, Zhu M, Comyn SA, Persaud A, Deshaies RJ, Rotin D, Gsponer J, Mayor T, Rsp5/Nedd4 is the main ubiquitin ligase that targets cytosolic misfolded proteins following heat stress. Nat Cell Biol, 16(12):1227-37(2014) [pubmed] |
10.1038/ncb3054; |
Keyword List
curator keyword: Biological |
submitter keyword: Rsp5, heat-shock, cytosolic protein quality control |
Contact List
Nancy Fang |
contact affiliation | Mayor Lab the Centre for High-Thoughput Biology Dept. of Biochemistry and Molecular Biology the University of British Columbia |
contact email | nancynfang@gmail.com |
lab head | |
Neng Fang |
contact affiliation | Centre for High Throughput Biology |
contact email | nengf@interchange.ubc.ca |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD001214
- Label: PRIDE project
- Name: Rsp5/Nedd4 is the major ubiquitin ligase that targets cytosolic misfolded proteins upon heat-stress