PXD042903 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Pulse-SILAC and interactomics reveal distinct DDB1-CUL4 associated factors (DCAFs), cellular functions, and protein substrates |
Description | Cullin-RING finger ligases (CRLs) represent the largest family of ubiquitin ligases. They are responsible for the ubiquitination of ~20% of cellular proteins degraded through the proteasome, by catalyzing the transfer of E2-loaded ubiquitin to a substrate. Seven Cullins are described in vertebrates. Among them, CUL4 associates with DDB1 to form the CUL4-DDB1 ubiquitin ligase complex, which is involved in protein ubiquitination and in the regulation of many cellular processes. Substrate recognition adaptors named DDB1/CUL4 associated factors (DCAF) mediate the specificity of CUL4-DDB1 and have a short structural motif of approximately forty amino acids terminating in a tryptophan (W)-aspartic acid (D) dipeptide, called the WD40 domain. Using different approaches (bioinformatics/structural analyses), independent studies suggested that at least sixty WD40-containing proteins could act as adaptors for the DDB1/CUL4 complex. To better define this association and classification, the interaction of each DCAFs with DDB1 was determined, and new partners and potential substrates were identified. Using BioID and AP-MS approaches, we demonstrated that seven WD40 proteins can be considered DCAFs with a high confidence level. Identifying protein interactions does not always lead to identifying protein substrates for E3-ubiquitin ligases, so we measured changes in protein stability or degradation by pulse-SILAC to identify changes in protein degradation following the expression of each DCAF. In conclusion, these results provide new insights into the roles of DCAFs in regulating the activity of the DDB1-CUL4 complex, in protein targeting, and characterized the cellular processes involved |
HostingRepository | PRIDE |
AnnounceDate | 2023-11-14 |
AnnouncementXML | Submission_2023-11-14_07:26:32.850.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Dominique Levesque |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | carbamoylated residue; monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2023-06-12 03:52:22 | ID requested | |
1 | 2023-10-11 10:41:24 | announced | |
⏵ 2 | 2023-11-14 07:26:33 | announced | 2023-11-14: Updated project metadata. |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: Pulse-SILAC, DCAFs, ubiquitination, BioID, DDB1, interactome, Cullin4 |
Contact List
Francois Michel Boisvert |
contact affiliation | Immonolgy and cell biology department, université de sherbrooke |
contact email | francois.michel.boisvert@usherbrooke.ca |
lab head | |
Dominique Levesque |
contact affiliation | University of Sherbrooke, FM Boisvert lab |
contact email | dominique.levesque@usherbrooke.ca |
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/2023/10/PXD042903 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD042903
- Label: PRIDE project
- Name: Pulse-SILAC and interactomics reveal distinct DDB1-CUL4 associated factors (DCAFs), cellular functions, and protein substrates