PXD042987 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Nuclear Hsp104 safeguards the dormant translation machinery during quiescence |
Description | The 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. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_06:21:45.571.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Ignasi Forne |
SpeciesList | scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932; |
ModificationList | No PTMs are included in the dataset |
Instrument | Orbitrap Exploris 480 |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2023-06-14 09:30:38 | ID requested | |
1 | 2024-01-11 23:57:03 | announced | |
⏵ 2 | 2024-10-22 06:21:45 | announced | 2024-10-22: Updated project metadata. |
Publication List
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 affiliation | Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, 10691 Stockholm, Sweden |
contact email | sabrina.buettner@su.se |
lab head | |
Ignasi Forne |
contact affiliation | Biomedical Center-LMU |
contact email | ignasi.forne@lrz.uni-muenchen.de |
dataset submitter | |
Full Dataset Link List
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/2024/01/PXD042987 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD042987
- Label: PRIDE project
- Name: Nuclear Hsp104 safeguards the dormant translation machinery during quiescence