{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kassmeier MD"],"funding":["NCRR NIH HHS","NIAID NIH HHS","NIMH NIH HHS","NIGMS NIH HHS"],"pagination":["945-58"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3280554"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["31(4)"],"pubmed_abstract":["The N-terminus of full-length RAG1, though dispensable for RAG1/2 cleavage activity, is required for efficient V(D)J recombination. This region supports RING E3 ubiquitin ligase activity in vitro, but whether full-length RAG1 functions as a single subunit or a multi-subunit E3 ligase in vivo is unclear. We show the multi-subunit cullin RING E3 ligase complex VprBP/DDB1/Cul4A/Roc1 associates with full-length RAG1 through VprBP. This complex is assembled into RAG protein-DNA complexes, and supports in-vitro ubiquitylation activity that is insensitive to RAG1 RING domain mutations. Conditional B lineage-specific VprBP disruption arrests B-cell development at the pro-B-to-pre-B cell transition, but this block is bypassed by expressing rearranged immunoglobulin transgenes. Mice with a condition"],"journal":["The EMBO journal"],"pubmed_title":["VprBP binds full-length RAG1 and is required for B-cell development and V(D)J recombination fidelity."],"pmcid":["PMC3280554"],"funding_grant_id":["1S10RR027352","R56 AI055599","AI055599","P30 MH062261","R56AI091748-01A1","R01 GM067113","G20 RR024001","R56 AI091748","S10 RR027352","R01 AI055599","G20RR024001"],"pubmed_authors":["Xiong Y","Raval P","Jackson S","Swanson PC","Kassmeier MD","Mondal K","Ciborowski P","Anderson DK","Palmer VL","Kumar S","Perry GA"],"additional_accession":[]},"is_claimable":false,"name":"VprBP binds full-length RAG1 and is required for B-cell development and V(D)J recombination fidelity.","description":"The N-terminus of full-length RAG1, though dispensable for RAG1/2 cleavage activity, is required for efficient V(D)J recombination. This region supports RING E3 ubiquitin ligase activity in vitro, but whether full-length RAG1 functions as a single subunit or a multi-subunit E3 ligase in vivo is unclear. We show the multi-subunit cullin RING E3 ligase complex VprBP/DDB1/Cul4A/Roc1 associates with full-length RAG1 through VprBP. This complex is assembled into RAG protein-DNA complexes, and supports in-vitro ubiquitylation activity that is insensitive to RAG1 RING domain mutations. Conditional B lineage-specific VprBP disruption arrests B-cell development at the pro-B-to-pre-B cell transition, but this block is bypassed by expressing rearranged immunoglobulin transgenes. Mice with a condition","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Feb","modification":"2025-04-26T21:01:15.903Z","creation":"2019-03-27T00:49:13Z"},"accession":"S-EPMC3280554","cross_references":{"pubmed":["22157821"],"doi":["10.1038/emboj.2011.455"]}}