CRL4(RBBP7) is required for efficient CENP-A deposition at centromeres.

Journal of Cell Science
Julien MouyssetMatthias Peter

Abstract

The mitotic spindle drives chromosome movement during mitosis and attaches to chromosomes at dedicated genomic loci named centromeres. Centromeres are epigenetically specified by their histone composition, namely the presence of the histone H3 variant CENP-A, which is regulated during the cell cycle by its dynamic expression and localization. Here, we combined biochemical methods and quantitative imaging approaches to investigate a new function of CUL4-RING E3 ubiquitin ligases (CRL4) in regulating CENP-A dynamics. We found that the core components CUL4 and DDB1 are required for centromeric loading of CENP-A, but do not influence CENP-A maintenance or pre-nucleosomal CENP-A levels. Interestingly, we identified RBBP7 as a substrate-specific CRL4 adaptor required for this process, in addition to its role in binding and stabilizing soluble CENP-A. Our data thus suggest that the CRL4 complex containing RBBP7 (CRL4(RBBP7)) might regulate mitosis by promoting ubiquitin-dependent loading of newly synthesized CENP-A during the G1 phase of the cell cycle.

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Citations

Mar 26, 2016·Differentiation; Research in Biological Diversity·Sami G Almalki, Devendra K Agrawal
Jan 11, 2017·Nucleus·Fabienne LampertMatthias Peter
Jul 8, 2017·The Journal of Cell Biology·Samuel Gilberto, Matthias Peter
Mar 10, 2018·Nucleic Acids Research·Geetha S HewawasamJennifer L Gerton
Oct 3, 2020·Experimental & Molecular Medicine·Sang-Min JangMirit I Aladjem
Aug 30, 2020·International Journal of Molecular Sciences·Hwei Ling TanEe Sin Chen

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