論文

査読有り
2017年1月

CDK-regulated dimerization of M18BP1 on a Mis 18 hexamer is necessary for CENP-A loading

ELIFE
  • Dongqing Pan
  • ,
  • Kerstin Klare
  • ,
  • Arsen Petrovic
  • ,
  • Annika Take
  • ,
  • Kai Walstein
  • ,
  • Priyanka Singh
  • ,
  • Arnaud Rondelet
  • ,
  • Alexander W. Bird
  • ,
  • Andrea Musacchio

6
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.7554/eLife.23352
出版者・発行元
ELIFE SCIENCES PUBLICATIONS LTD

Centromeres are unique chromosomal loci that promote the assembly of kinetochores, macromolecular complexes that bind spindle microtubules during mitosis. In most organisms, centromeres lack defined genetic features. Rather, they are specified epigenetically by a centromere-specific histone H3 variant, CENP-A. The Mis18 complex, comprising the Mis18a:Mis18 subcomplex and M18BP1, is crucial for CENP-A homeostasis. It recruits the CENP-A-specific chaperone HJURP to centromeres and primes it for CENP-A loading. We report here that a specific arrangement of Yippee domains in a human Mis18 alpha:Mis18 beta 4:2 hexamer binds two copies of M18BP1 through M18BP1s 140 N-terminal residues. Phosphorylation by Cyclin-dependent kinase 1 (CDK1) at two conserved sites in this region destabilizes binding to Mis18 alpha:Mis18 beta, limiting complex formation to the G1 phase of the cell cycle. Using an improved viral 2A peptide co-expression strategy, we demonstrate that CDK1 controls Mis18 complex recruitment to centromeres by regulating oligomerization of M18BP1 through the Mis18 alpha:Mis18 beta scaffold.


リンク情報
DOI
https://doi.org/10.7554/eLife.23352
Scopus
https://www.scopus.com/record/display.uri?eid=2-s2.0-85010689280&origin=inward
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000393400000001&DestApp=WOS_CPL
URL
http://www.scopus.com/inward/record.url?eid=2-s2.0-85010689280&partnerID=MN8TOARS
URL
http://orcid.org/0000-0003-3701-8442