2020/08/19 by Mònica Torras‐Llort, Sònia Medina-Giró, Paula Escudero-Ferruz +5 · 1 voice
Biochemistry, Genetics and Molecular Biology · #Genomics and Chromatin Dynamics #Nuclear Structure and Function #RNA Research and Splicing
paper · pdf · doi:10.1038/s42003-020-01182-y
openalex publication_date 2020/08/19 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01
Barrier-to-Autointegration Factor (BAF) is a conserved nuclear envelope (NE) component that binds chromatin and helps its anchoring to the NE. Cycles of phosphorylation and dephosphorylation control BAF function. Entering mitosis, phosphorylation releases BAF from chromatin and facilitates NE-disassembly. At mitotic exit, PP2A-mediated dephosphorylation restores chromatin binding and nucleates NE-reassembly. Here, we show that in Drosophila a small fraction of BAF (cenBAF) associates with centromeres. We also find that PP4 phosphatase, which is recruited to centromeres by CENP-C, prevents phosphorylation and release of cenBAF during mitosis. cenBAF is necessary for proper centromere assembly and accurate chromosome segregation, being critical for mitosis progression. Disrupting cenBAF localization prevents PP2A inactivation in mitosis compromising global BAF phosphorylation, which in turn leads to its persistent association with chromatin, delays anaphase onset and causes NE defects. These results suggest that, together with PP4 and CENP-C, cenBAF forms a centromere-based mechanism that controls chromosome segregation and mitosis progression.