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PXD042987

PXD042987 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleNuclear Hsp104 safeguards the dormant translation machinery during quiescence
DescriptionThe resilience of cellular proteostasis declines with age, which drives protein aggregation and compromises viability. The nucleus has emerged as a key quality control compartment that unloads the cytosolic protein biosynthesis system from misfolded proteins. Here, we find that age-associated metabolic cues target the yeast protein disaggregase Hsp104 to the nucleus to maintain a functional nuclear proteome during quiescence. The switch to respiratory metabolism and the accompanying decrease in translation rates direct cytosolic Hsp104 to the nucleus to interact with latent translation initiation factor eIF2 subcomplexes and to suppress protein aggregation. Hindering Hsp104 from entering the nucleus in quiescent cells results in delayed re-entry into the cell cycle due to compromised resumption of protein synthesis. In sum, we report that cytosolic-nuclear partitioning of the Hsp104 disaggregase is a critical mechanism to protect the latent protein synthesis machinery during quiescence, ensuring the rapid restart of translation once nutrients are replenished.
HostingRepositoryPRIDE
AnnounceDate2024-10-22
AnnouncementXMLSubmission_2024-10-22_06:21:45.571.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterIgnasi Forne
SpeciesList scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationListNo PTMs are included in the dataset
InstrumentOrbitrap Exploris 480
Dataset History
RevisionDatetimeStatusChangeLog Entry
02023-06-14 09:30:38ID requested
12024-01-11 23:57:03announced
22024-10-22 06:21:45announced2024-10-22: Updated project metadata.
Publication List
10.1038/S41467-023-44538-8;
Keyword List
submitter keyword: Quiescence, eIF2, Aging, Nuclear protein quality control, Protein aggregation,Disaggregation, Translation, Proteasome, Hsp104, Ribosome reactivation, BioID
Contact List
Sabrina Büttner
contact affiliationDepartment of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, 10691 Stockholm, Sweden
contact emailsabrina.buettner@su.se
lab head
Ignasi Forne
contact affiliationBiomedical Center-LMU
contact emailignasi.forne@lrz.uni-muenchen.de
dataset submitter
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Dataset FTP location
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