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http://purl.uniprot.org/citations/17199038http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17199038http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17199038http://www.w3.org/2000/01/rdf-schema#comment"The centromere is the chromosomal site that joins to microtubules during mitosis for proper segregation. Determining the location of a centromere-specific histone H3 called CENP-A at the centromere is vital for understanding centromere structure and function. Here, we report the identification of three human proteins essential for centromere/kinetochore structure and function, hMis18alpha, hMis18beta, and M18BP1, the complex of which is accumulated specifically at the telophase-G1 centromere. We provide evidence that such centromeric localization of hMis18 is essential for the subsequent recruitment of de novo-synthesized CENP-A. If any of the three is knocked down by RNAi, centromere recruitment of newly synthesized CENP-A is rapidly abolished, followed by defects such as misaligned chromosomes, anaphase missegregation, and interphase micronuclei. Tricostatin A, an inhibitor to histone deacetylase, suppresses the loss of CENP-A recruitment to centromeres in hMis18alpha RNAi cells. Telophase centromere chromatin may be primed or licensed by the hMis18 complex and RbAp46/48 to recruit CENP-A through regulating the acetylation status in the centromere."xsd:string
http://purl.uniprot.org/citations/17199038http://purl.org/dc/terms/identifier"doi:10.1016/j.devcel.2006.11.002"xsd:string
http://purl.uniprot.org/citations/17199038http://purl.org/dc/terms/identifier"doi:10.1016/j.devcel.2006.11.002"xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/author"Fujita Y."xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/author"Fujita Y."xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/author"Hayashi T."xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/author"Hayashi T."xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/author"Toyoda Y."xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/author"Toyoda Y."xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/author"Yanagida M."xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/author"Yanagida M."xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/author"Kiyomitsu T."xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/author"Kiyomitsu T."xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/author"Obuse C."xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/author"Obuse C."xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/author"Kokubu A."xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/author"Kokubu A."xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/name"Dev. Cell"xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/name"Dev. Cell"xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/pages"17-30"xsd:string
http://purl.uniprot.org/citations/17199038http://purl.uniprot.org/core/pages"17-30"xsd:string