biostudies-literatureMarcelot AiNEXTFrench Infrastructure for Integrated Structural BiologyEC Seventh Framework Programme3841-3855https://www.ebi.ac.uk/biostudies/studies/S-EPMC8053085biostudies-literatureUnknown49(7)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 strucNucleic acids researchDi-phosphorylated BAF shows altered structural dynamics and binding to DNA, but interacts with its nuclear envelope partners.PMC8053085653706ANR-10-INSB-05-01871037Marcelot ATheillet FXDubois SZinn-Justin SMiron SSamson CHoffmann GThai RPetitalot AMarquez JARopars VLe Du MHCuniasse PfalseDi-phosphorylated BAF shows altered structural dynamics and binding to DNA, but interacts with its nuclear envelope partners.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 struc2021-01-01T00:00:00Z2021 Apr2026-04-07T16:56:43.658Z2022-02-10T18:53:30.135ZS-EPMC80530853374494110.1093/nar/gkab184