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XB-ART-44037
J Cell Biol September 19, 2011; 194 (6): 855-71.

CENP-C recruits M18BP1 to centromeres to promote CENP-A chromatin assembly.

Moree B , Meyer CB , Fuller CJ , Straight AF .


Abstract
Eukaryotic chromosomes segregate by attaching to microtubules of the mitotic spindle through a chromosomal microtubule binding site called the kinetochore. Kinetochores assemble on a specialized chromosomal locus termed the centromere, which is characterized by the replacement of histone H3 in centromeric nucleosomes with the essential histone H3 variant CENP-A (centromere protein A). Understanding how CENP-A chromatin is assembled and maintained is central to understanding chromosome segregation mechanisms. CENP-A nucleosome assembly requires the Mis18 complex and the CENP-A chaperone HJURP. These factors localize to centromeres in telophase/G1, when new CENP-A chromatin is assembled. The mechanisms that control their targeting are unknown. In this paper, we identify a mechanism for recruiting the Mis18 complex protein M18BP1 to centromeres. We show that depletion of CENP-C prevents M18BP1 targeting to metaphase centromeres and inhibits CENP-A chromatin assembly. We find that M18BP1 directly binds CENP-C through conserved domains in the CENP-C protein. Thus, CENP-C provides a link between existing CENP-A chromatin and the proteins required for new CENP-A nucleosome assembly.

PubMed ID: 21911481
PMC ID: PMC3207292
Article link: J Cell Biol
Grant support: [+]
Genes referenced: anln cenpa cenpc h4c4 mis18bp1 myc tab3 wee1
Antibodies: Cenpa Ab1 Cenpc1 Ab1 Hist1h4a Ab2 Mis18bp1 Ab1


Article Images: [+] show captions
References [+] :
Allshire, Epigenetic regulation of centromeric chromatin: old dogs, new tricks? 2008, Pubmed


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