{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["16(1)"],"submitter":["Wu X"],"pubmed_abstract":["The K29/K48-linked ubiquitination generated by the cooperative catalysis of E3 ligase Ufd4 and Ubr1 is an enhanced protein degradation signal, in which Ufd4 is responsible for introducing K29-linked ubiquitination to K48-linked ubiquitin chains to augment polyubiquitination. How HECT-E3 ligase Ufd4 mediates the ubiquitination event remains unclear. Here, we biochemically determine that Ufd4 preferentially catalyses K29-linked ubiquitination on K48-linked ubiquitin chains to generate K29/K48-branched ubiquitin chains and capture structural snapshots of Ub transfer cascades for Ufd4-mediated ubiquitination. The N-terminal ARM region and HECT domain C-lobe of Ufd4 are identified and characterized as key structural elements that together recruit K48-linked diUb and orient Lys29 of its proximal"],"journal":["Nature communications"],"pagination":["4313"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12062229"],"repository":["biostudies-literature"],"pubmed_title":["Structural visualization of HECT-type E3 ligase Ufd4 accepting and transferring ubiquitin to form K29/K48-branched polyubiquitination."],"pmcid":["PMC12062229"],"pubmed_authors":["Liu L","Tong Z","Deng Z","Liang LJ","Zheng Q","Cai H","Wu X","Ai H","Mao J","Pan M"],"additional_accession":[]},"is_claimable":false,"name":"Structural visualization of HECT-type E3 ligase Ufd4 accepting and transferring ubiquitin to form K29/K48-branched polyubiquitination.","description":"The K29/K48-linked ubiquitination generated by the cooperative catalysis of E3 ligase Ufd4 and Ubr1 is an enhanced protein degradation signal, in which Ufd4 is responsible for introducing K29-linked ubiquitination to K48-linked ubiquitin chains to augment polyubiquitination. How HECT-E3 ligase Ufd4 mediates the ubiquitination event remains unclear. Here, we biochemically determine that Ufd4 preferentially catalyses K29-linked ubiquitination on K48-linked ubiquitin chains to generate K29/K48-branched ubiquitin chains and capture structural snapshots of Ub transfer cascades for Ufd4-mediated ubiquitination. The N-terminal ARM region and HECT domain C-lobe of Ufd4 are identified and characterized as key structural elements that together recruit K48-linked diUb and orient Lys29 of its proximal","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 May","modification":"2026-06-02T12:09:09.324Z","creation":"2026-04-18T03:11:07.396Z"},"accession":"S-EPMC12062229","cross_references":{"pubmed":["40341121"],"doi":["10.1038/s41467-025-59569-6"]}}