PXD024791 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | The C-terminus of the PSMA3 proteasome subunit preferentially traps intrinsically disordered proteins for degradation |
Description | Degradation of intrinsically disordered proteins (IDPs) by a non-26S proteasome process does not require proteasomal targeting by polyubiquitin. However, whether and how IDPs are recognized by the non-26S proteasome, including the 20S complex, remains unknown. Analyses of protein interactome datasets revealed that the 20S proteasome subunit, PSMA3, preferentially interacts with many IDPs. Employing in vivo and cell-free experiments, it was found that a 69-amino-acids-long fragment at the C-terminus of PSMA3 is sufficient to bind the disordered protein p21. A recombinant PSMA3 C-terminus 69 fragment is sufficient to interact with many IDPs, and is therefore designated an IDP trapper. A recombinant IDP trapper blocks the degradation of many IDPs in vitro by the 20S proteasome, possibly by competing with the native trapper. In addition, over a third of the PSMA3 trapper-binding proteins have previously been identified as 20S proteasome substrates, and based on published datasets many of the trapper binding proteins are associated with the intracellular proteasomes. The PSMA3-trapped IDPs that are proteasome substrates have the unique features previously recognized as characteristic 20S proteasome substrates in vitro. We propose a model whereby the PSMA3 C-terminal region traps a subset of IDPs to facilitate their proteasomal degradation. |
HostingRepository | PRIDE |
AnnounceDate | 2023-11-14 |
AnnouncementXML | Submission_2023-11-14_08:35:54.132.xml |
DigitalObjectIdentifier | https://dx.doi.org/10.6019/PXD024791 |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | Yishai Levin |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive Plus |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2021-03-17 04:42:35 | ID requested | |
1 | 2023-03-10 19:41:15 | announced | |
⏵ 2 | 2023-11-14 08:35:54 | announced | 2023-11-14: Updated project metadata. |
Publication List
10.6019/PXD024791; |
Biran A, Myers N, Steinberger S, Adler J, Riutin M, Broennimann K, Reuven N, Shaul Y, The C-Terminus of the PSMA3 Proteasome Subunit Preferentially Traps Intrinsically Disordered Proteins for Degradation. Cells, 11(20):(2022) [pubmed] |
Keyword List
submitter keyword: proteasome, disordered proteins, proteomics |
Contact List
Yosef Shaul |
contact affiliation | Weizmann Institute of Science |
contact email | yosef.shaul@weizmann.ac.il |
lab head | |
Yishai Levin |
contact affiliation | Weizmann Institute of Science, Israel |
contact email | yishai.levin@gmail.com |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD024791
- Label: PRIDE project
- Name: The C-terminus of the PSMA3 proteasome subunit preferentially traps intrinsically disordered proteins for degradation