Literature DB >> 25727006

CENP-A K124 Ubiquitylation Is Required for CENP-A Deposition at the Centromere.

Yohei Niikura1, Risa Kitagawa1, Hiroo Ogi1, Rashid Abdulle1, Vishwajeeth Pagala2, Katsumi Kitagawa3.   

Abstract

CENP-A is a centromere-specific histone H3 variant that epigenetically determines centromere identity to ensure kinetochore assembly and proper chromosome segregation, but the precise mechanism of its specific localization within centromeric heterochromatin remains obscure. We have discovered that CUL4A-RBX1-COPS8 E3 ligase activity is required for CENP-A ubiquitylation on lysine 124 (K124) and CENP-A centromere localization. A mutation of CENP-A, K124R, reduces interaction with HJURP (a CENP-A-specific histone chaperone) and abrogates localization of CENP-A to the centromere. Addition of monoubiquitin is sufficient to restore CENP-A K124R to centromeres and the interaction with HJURP, indicating that "signaling" ubiquitylation is required for CENP-A loading at centromeres. The CUL4A-RBX1 complex is required for loading newly synthesized CENP-A and maintaining preassembled CENP-A at centromeres. Thus, CENP-A K124R ubiquitylation, mediated by the CUL4A-RBX1-COPS8 complex, is essential for CENP-A deposition at the centromere.
Copyright © 2015 Elsevier Inc. All rights reserved.

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Year:  2015        PMID： 25727006      PMCID： PMC4374629          DOI： 10.1016/j.devcel.2015.01.024

Source DB:  PubMed          Journal:  Dev Cell        ISSN： 1534-5807            Impact factor:   12.270


  64 in total

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  47 in total

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10.  A JUMONJI Protein with E3 Ligase and Histone H3 Binding Activities Affects Transposon Silencing in Arabidopsis.

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