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PXD002202

PXD002202 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleUbiquitin S65 proteomics: Association of ubiquitin mutants with ubiqiutin binding domains
DescriptionUbiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be phosphorylated. However, the effect of this modification on ubiquitin function is largely unknown. Here, we performed in vivo and in vitro characterization of the effects of phosphorylation of yeast ubiquitin at position serine 65. We find ubiquitin S65 phosphorylation to be regulated under oxidative stress, occurring in tandem with the restructuring of the ubiquitin landscape into a highly polymeric state. Phosphomimetic mutation of S65 recapitulates the oxidative stress phenotype, causing a dramatic accumulation of ubiquitylated proteins and a proteome-wide reduction of protein turnover rates. Importantly, this mutation impacts ubiquitin chain disassembly, chain linkage distribution, and substrate targeting. These results demonstrate that phosphorylation represents an additional mode of ubiquitin regulation with broad implications in cellular physiology.
HostingRepositoryPRIDE
AnnounceDate2015-07-11
AnnouncementXMLSubmission_2015-07-11_00:31:50.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterDanielle Swaney
SpeciesList scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationListNo PTMs are included in the dataset
InstrumentLTQ Orbitrap Velos
Dataset History
RevisionDatetimeStatusChangeLog Entry
02015-05-19 02:14:07ID requested
12015-07-08 01:55:02announced
22015-07-11 00:31:51announcedUpdated project metadata.
Publication List
Swaney DL, Rodr, í, guez-Mias RA, Vill, é, n J, Phosphorylation of ubiquitin at Ser65 affects its polymerization, targets, and proteome-wide turnover. EMBO Rep, 16(9):1131-44(2015) [pubmed]
Keyword List
curator keyword: Biological
submitter keyword: Yeast, ubiquitin, phosphorylation, orbitrap
Contact List
Judit Villen
contact affiliationUniversity of Washington
contact emailjvillen@uw.edu
lab head
Danielle Swaney
contact affiliationUCSF
contact emaildaniswan@gmail.com
dataset submitter
Full Dataset Link List
Dataset FTP location
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PRIDE project URI
Repository Record List
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