| Literature DB >> 30016453 |
Saima Akram1, Fengrui Yang1,2, Junying Li1, Gregory Adams2,3, Yingying Liu1,2, Xiaoxuan Zhuang1,3, Lingluo Chu4, Xu Liu1,2, Nerimah Emmett2, Winston Thompson2, McKay Mullen2, Saravana Muthusamy2, Wenwen Wang1,2, Fei Mo1,3, Xing Liu1,2.
Abstract
Heterochromatin protein 1α (HP1α) regulates chromatin specification and plasticity during cell fate decision. Different structural determinants account for HP1α localization and function during cell division cycle. Our earlier study showed that centromeric localization of HP1α 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 HP1α to the centromere of mitotic chromosomes and its interaction with HP1α is essential for accurate chromosome segregation during mitosis. LRIF1 interacts directly with HP1α chromoshadow domain via an evolutionarily conserved PXVXL motif within its C-terminus. Importantly, the LRIF1-HP1α interaction is critical for Aurora B activity in the inner centromere. Mutation of PXVXL motif of LRIF1 leads to defects in HP1α centromere targeting and aberrant chromosome segregation. These findings reveal a previously unrecognized direct link between LRIF1 and HP1α in centromere plasticity control and illustrate the critical role of LRIF1-HP1α interaction in orchestrating accurate cell division.Entities:
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Year: 2018 PMID： 30016453 PMCID： PMC6304163 DOI： 10.1093/jmcb/mjy040
Source DB: PubMed Journal: J Mol Cell Biol ISSN： 1759-4685 Impact factor: 6.216