PXD001214

PXD001214 is an original dataset announced via ProteomeXchange.

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

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.

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;

curator keyword: Biological

submitter keyword: Rsp5, heat-shock, cytosolic protein quality control

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

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2016/07/PXD001214

PRIDE project URI

• PRIDE
  1. PXD001214
     1. Label: PRIDE project
     2. Name: Rsp5/Nedd4 is the major ubiquitin ligase that targets cytosolic misfolded proteins upon heat-stress