PXD004747-2

PXD004747 is an original dataset announced via ProteomeXchange.

Title	Deubiquitinase activity is required for the degradation of misfolded cytosolic proteins upon heat-stress
Description	Elimination of misfolded proteins is crucial for proteostasis and to prevent proteinopathies. Nedd4/Rsp5 emerged as a major E3 ligase involved in multiple quality control pathways that target misfolded plasma membrane proteins, aggregated polypeptides, and cytosolic heat-induced misfolded proteins for degradation. It remained unclear how in one case cytosolic heat-induced Rsp5 substrates are destined for proteasomal degradation, whereas other Rsp5 quality control substrates are otherwise directed to lysosomal degradation. Here we find that Ubp2 and Ubp3 deubiquitinases are required for the proteasomal degradation of cytosolic misfolded proteins targeted by Rsp5 after heat-shock. The two deubiquitinases associate more with Rsp5 upon heat stress to prevent the assembly of K63-linked ubiquitin on Rsp5 heat-induced substrates. This activity was required to promote the K48-mediated proteasomal degradation of Rsp5 heat-shock induced substrates. Our results indicate that ubiquitin chain editing is key to the cytosolic protein quality control under stress conditions.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:34:48.325.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	ubiquitination signature dipeptidyl lysine; phosphorylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	6460 Triple Quadrupole LC/MS; LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2016-08-10 03:20:54	ID requested
1	2022-03-01 13:19:13	announced
⏵ 2	2024-10-22 05:34:50	announced	2024-10-22: Updated project metadata.

Fang NN, Zhu M, Rose A, Wu KP, Mayor T, Deubiquitinase activity is required for the proteasomal degradation of misfolded cytosolic proteins upon heat-stress. Nat Commun, 7():12907(2016) [pubmed]

10.1038/ncomms12907;

curator keyword: Biological

submitter keyword: Deubiquitinase, cytosolic protein quality control, heat stress

Thibault Mayor
contact affiliation	Associate Professor, Mayor Lab, Department of Biochemistry and Molecular Biology, Michael Smith Laboratories, University of British Columbia, 2125 East Mall, Vancouver, BC V6T1Z4, Canada
contact email	mayor@mail.ubc.ca
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/2022/03/PXD004747

PRIDE project URI

• PRIDE
  1. PXD004747
     1. Label: PRIDE project
     2. Name: Deubiquitinase activity is required for the degradation of misfolded cytosolic proteins upon heat-stress