LRIF1 interacts with HP1? to coordinate accurate chromosome segregation during mitosis.

ABSTRACT: Heterochromatin protein 1? (HP1?) regulates chromatin specification and plasticity during cell fate decision. Different structural determinants account for HP1? localization and function during cell division cycle. Our earlier study showed that centromeric localization of HP1? depends on the epigenetic mark H3K9me3 in interphase, while its centromeric location in mitosis relies on uncharacterized PXVXL-containing factors. Here, we identified a PXVXL-containing protein, ligand-dependent nuclear receptor-interacting factor 1 (LRIF1), which recruits HP1? to the centromere of mitotic chromosomes and its interaction with HP1? is essential for accurate chromosome segregation during mitosis. LRIF1 interacts directly with HP1? chromoshadow domain via an evolutionarily conserved PXVXL motif within its C-terminus. Importantly, the LRIF1-HP1? interaction is critical for Aurora B activity in the inner centromere. Mutation of PXVXL motif of LRIF1 leads to defects in HP1? centromere targeting and aberrant chromosome segregation. These findings reveal a previously unrecognized direct link between LRIF1 and HP1? in centromere plasticity control and illustrate the critical role of LRIF1-HP1? interaction in orchestrating accurate cell division.

SUBMITTER: Akram S 

PROVIDER: S-EPMC6304163 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature