{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070424/20080_L8B1_deadxlink_2.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070424/20080_L8B1_crosslink_1.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070424/20080_L8B1_dsshydrolysed_2.msf"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070424/checksum.txt"],"Mzml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070424/20080_L8B1_crosslink_1.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070424/20080_L8B1_crosslink_centroid.mzML"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070424/20080_L8B1_crosslink_1.RAW"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["catherine.day@otago.ac.nz"],"submitter":["Torsten Kleffmann"],"technology_type":["Mass Spectrometry","Chemical cross-linking coupled with mass spectrometry proteomics"],"software":["Not available"],"submitter_keywords":["Znrf3 e3 ligase","Cross-linking","Ring dimerization"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070424"],"tissue":["Cell Culture"],"sample_protocol":["BS3-d0 (21590 Thermo Fisher) were used for the lysine cross-linking experiments. Stock BS3-d0 (0.5 M) was prepared using DMSO and working concentrations were diluted into a buffer containing Tris 20 mM and 150 mM NaCl. The protein was mixed with the crosslinker at a 1:10 ratio of protein:BS3-d0 linker and incubated at 25°C for the indicated periods in a buffer containing 20 mM Tris pH 7.5 and 150 mM NaCl.  The cross-linked proteins were resolved on SDS PAGE gels and cut out for mass spectrometry. The proteins were digested with chymotrypsin using an in-gel approach. The resulting peptides were subjected to nanoflow liquid chromatography coupled tandem mass spectrometry (LC-MS/MS) using an Ultimate 3000 nano-flow uHPLC System inline coupled to an LTQ Orbitrap XL mass spectrometer (Thermo Scientific)."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["BS3-d0 cross-linked peptides were identified by searching the MS raw data against an inhouse database containing the target protein sequences using the StavroX3.6 software. Significant spectrum matches to cross-linked peptides were assessed manually for correct peak assignment."],"omics_type":["Proteomics"],"labhead":["Professor Catherine Day"],"instrument_platform":[""],"labhead_affiliation":["Department of Biochemistry, University of Otago, New Zealand"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["42378331 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. 2026 19(944):eaeb3656 10.1126/scisignal.aeb3656"],"submitter_mail":["torsten.kleffmann@otago.ac.nz"],"submitter_affiliation":["Department of Biochemistry, University of Otago"],"submitter_country":["New Zealand"],"pubmed_abstract":["The WNT signaling pathway regulates cell proliferation and stem cell maintenance. Its sustained and inappropriate activation results in excessive cell division and cancer. WNT signaling is activated upon interaction of the soluble WNT ligand with the Frizzled (FZD) receptor. The RING E3 ubiquitin ligases RNF43 and ZNRF3 promote the ubiquitylation and internalization of FZD, thereby turning off WNT signaling, and their inactivation causes cancer. Here, we identified the determinants of ubiquitin transfer by ZNRF3 and RNF43 and report the structure of the RING domain from ZNRF3. We found that the RING domain was monomeric and that RING dimerization was not required for its ubiquitin ligase activity. However, the ectodomain of ZNRF3 dimerizes, and our data supported a model in which the cytoplasmic domains are in close proximity in cells and interact, even though RING dimerization was not required for ubiquitin transfer. Our studies provide a framework for understanding how the E3 ubiquitin ligase activity of ZNRF3 and RNF43 is regulated."],"pubmed_title":["ZNRF3 and RNF43 are active monomeric E3 ubiquitin ligases that self-associate."],"pubmed_authors":["Padala Prasanth P, Rossig Claudia C, Crowther Jennifer M JM, Dobson Renwick C J RCJ, Patel Monica M, Kumar Abhishek A, Kleffmann Torsten T, Middleton Adam J AJ, Day Catherine L CL"],"additional_accession":[]},"is_claimable":false,"name":"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 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