PXD070424 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | ZNRF3 and RNF43 are active monomeric E3 ligases that self-associate |
| Description | Crosslinking mass spectrometry was used to identify the site of dimerization in the RING domain of ZNRF3. The two proteins, ZNRF3 and RNF43 have a key role in regulating the number of Frizzled (FZD) receptor on cells and their inactivation causes cancer. This is because they are RING E3 ligases that promote the ubiquitylation and internalisation of FZD, thereby turning off WNT signalling. Here we identify the key determinants of ubiquitin transfer by ZNRF3 and RNF43 and report the structure of the RING domain from ZNRF3. Our data indicate that the RING domain is monomeric, and that RING dimerization is not required for its ubiquitin ligase activity. However, the ectodomain of ZNRF3 forms dimers and our data supports a model where the cytoplasmic domains self-associate in cells even though RING dimerization is not required for activity. |
| HostingRepository | PRIDE |
| AnnounceDate | 2026-07-30 |
| AnnouncementXML | Submission_2026-07-30_13:14:10.968.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Torsten Kleffmann |
| SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606; |
| ModificationList | No PTMs are included in the dataset |
| Instrument | LTQ Orbitrap |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
|---|
| 0 | 2025-11-06 16:23:00 | ID requested | |
| ⏵ 1 | 2026-07-30 13:14:11 | announced | |
Publication List
| 10.1126/scisignal.aeb3656; |
| Padala P, Rossig C, Crowther JM, Dobson RCJ, Patel M, Kumar A, Kleffmann T, Middleton AJ, Day CL, ZNRF3 and RNF43 are active monomeric E3 ubiquitin ligases that self-associate. Sci Signal, 19(944):eaeb3656(2026) [pubmed] |
Keyword List
| submitter keyword: ZNRF3 E3 ligase,cross-linking, RING dimerization |
Contact List
| Professor Catherine Day |
|---|
| contact affiliation | Department of Biochemistry, University of Otago, New Zealand |
| contact email | catherine.day@otago.ac.nz |
| lab head | |
| Torsten Kleffmann |
|---|
| contact affiliation | Department of Biochemistry, University of Otago |
| contact email | torsten.kleffmann@otago.ac.nz |
| 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/2026/07/PXD070424 |
| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD070424
- Label: PRIDE project
- Name: ZNRF3 and RNF43 are active monomeric E3 ligases that self-associate
