{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Marcelot A"],"funding":["iNEXT","French Infrastructure for Integrated Structural Biology","EC Seventh Framework Programme"],"pagination":["3841-3855"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8053085"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["49(7)"],"pubmed_abstract":["Barrier-to-autointegration factor (BAF), encoded by the BANF1 gene, is an abundant and ubiquitously expressed metazoan protein that has multiple functions during the cell cycle. Through its ability to cross-bridge two double-stranded DNA (dsDNA), it favours chromosome compaction, participates in post-mitotic nuclear envelope reassembly and is essential for the repair of large nuclear ruptures. BAF forms a ternary complex with the nuclear envelope proteins lamin A/C and emerin, and its interaction with lamin A/C is defective in patients with recessive accelerated aging syndromes. Phosphorylation of BAF by the vaccinia-related kinase 1 (VRK1) is a key regulator of BAF localization and function. Here, we demonstrate that VRK1 successively phosphorylates BAF on Ser4 and Thr3. The crystal struc"],"journal":["Nucleic acids research"],"pubmed_title":["Di-phosphorylated BAF shows altered structural dynamics and binding to DNA, but interacts with its nuclear envelope partners."],"pmcid":["PMC8053085"],"funding_grant_id":["653706","ANR-10-INSB-05-01","871037"],"pubmed_authors":["Marcelot A","Theillet FX","Dubois S","Zinn-Justin S","Miron S","Samson C","Hoffmann G","Thai R","Petitalot A","Marquez JA","Ropars V","Le Du MH","Cuniasse P"],"additional_accession":[]},"is_claimable":false,"name":"Di-phosphorylated BAF shows altered structural dynamics and binding to DNA, but interacts with its nuclear envelope partners.","description":"Barrier-to-autointegration factor (BAF), encoded by the BANF1 gene, is an abundant and ubiquitously expressed metazoan protein that has multiple functions during the cell cycle. Through its ability to cross-bridge two double-stranded DNA (dsDNA), it favours chromosome compaction, participates in post-mitotic nuclear envelope reassembly and is essential for the repair of large nuclear ruptures. BAF forms a ternary complex with the nuclear envelope proteins lamin A/C and emerin, and its interaction with lamin A/C is defective in patients with recessive accelerated aging syndromes. Phosphorylation of BAF by the vaccinia-related kinase 1 (VRK1) is a key regulator of BAF localization and function. Here, we demonstrate that VRK1 successively phosphorylates BAF on Ser4 and Thr3. The crystal struc","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Apr","modification":"2026-04-07T16:56:43.658Z","creation":"2022-02-10T18:53:30.135Z"},"accession":"S-EPMC8053085","cross_references":{"pubmed":["33744941"],"doi":["10.1093/nar/gkab184"]}}