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PXD039550

PXD039550 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleIdentification of Zuo1 interactors upon rapamycin stress
DescriptionProteostasis is tightly regulated by TORC1 to meet cellular requirements. Upon TORC1 inhibition, degradative activity is increased, and protein synthesis is reduced through inhibition of translation initiation, to maintain cell viability. Here, we show that the ribosome-associated complex (RAC)/Ssb chaperone system is required to maintain proteostasis and cell viability under TORC1 inhibition, in yeast. In the absence of the Hsp40 cochaperone Zuo1, translation does not decrease in response to loss of TORC1 activity. The functional interaction between Zuo1 and its Hsp70 partner, Ssb is required for proper translational control and proteostasis maintenance upon TORC1 inhibition. Further, we have found that the rapid degradation of eIF4G following TORC1 inhibition is prevented in zuo1Δ cells, contributing to decreased survival in these conditions. Our findings suggest a new role for RAC/Ssb in regulating translation in response to changes in TORC1 signalling.
HostingRepositoryPRIDE
AnnounceDate2023-11-14
AnnouncementXMLSubmission_2023-11-14_08:29:54.203.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterFrederic Lamoliatte
SpeciesList scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationListmonohydroxylated residue; iodoacetamide derivatized residue
InstrumentOrbitrap Fusion
Dataset History
RevisionDatetimeStatusChangeLog Entry
02023-01-18 16:26:56ID requested
12023-09-11 04:07:51announced
22023-11-14 08:29:54announced2023-11-14: Updated project metadata.
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: LC-MSMS,Yeast, TMT-labelling, Immunoprecipitation, Co-chaperones
Contact List
Adrien Rousseau
contact affiliationMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, Scotland
contact emaila.rousseau@dundee.ac.uk
lab head
Frederic Lamoliatte
contact affiliationUniversity of Dundee
contact emailflamoliatte001@dundee.ac.uk
dataset submitter
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Dataset FTP location
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