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  • 1
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    CDK phosphorylation of Xenopus laevis M18BP1 promotes its metaphase centromere localization (2019)
    Springer Nature
    Details
    Publication Date: 2019
    Description: 〈sec〉〈st〉Synopsis〈/st〉〈p〉〈textbox textbox-type="graphic"〉〈p〉〈inline-fig〉〈/inline-fig〉〈/p〉〈/textbox〉〈/p〉 〈p〉Epigenetic specification of vertebrate centromeres depends on assembly of CENP-A nucleosomes during interphase. In frogs, phosphorylation-dependent targeting of the CENP-A recruitment factor M18BP1 already during mitosis is crucial for its later nuclear localization and assembly role.〈/p〉 〈p〉 〈l type="unord"〉〈li〉〈p〉CDK phosphorylation on 〈i〉Xenopus laevis〈/i〉 M18BP1 is required for its interaction with CENP-C in metaphase.〈/p〉〈/li〉 〈li〉〈p〉Mutations that disrupt metaphase M18BP1 localization result in defective interphase localization and CENP-A assembly.〈/p〉〈/li〉 〈li〉〈p〉M18BP1 exchange across the nuclear envelope is limited.〈/p〉〈/li〉 〈li〉〈p〉Metaphase M18BP1 localization may promote its retention on chromatin during nuclear envelope assembly.〈/p〉〈/li〉〈/l〉 〈/p〉〈/sec〉
    Print ISSN: 0261-4189
    Electronic ISSN: 1460-2075
    Topics: Biology , Medicine
    Published by Springer Nature on behalf of The European Molecular Biology Organization (EMBO).
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  • 2
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    CDK phosphorylation of Xenopus laevis M18BP1 promotes its metaphase centromere localization (2019)
    Springer Nature
    Details
    Publication Date: 2019
    Description: 〈p〉Chromosome segregation requires the centromere, the site on chromosomes where kinetochores assemble in mitosis to attach chromosomes to the mitotic spindle. Centromere identity is defined epigenetically by the presence of nucleosomes containing the histone H3 variant CENP-A. New CENP-A nucleosome assembly occurs at the centromere every cell cycle during G1, but how CENP-A nucleosome assembly is spatially and temporally restricted remains poorly understood. Centromere recruitment of factors required for CENP-A assembly is mediated in part by the three-protein Mis18 complex (Mis18α, Mis18β, M18BP1). Here, we show that 〈i〉Xenopus〈/i〉 M18BP1 localizes to centromeres during metaphase—prior to CENP-A assembly—by binding to CENP-C using a highly conserved SANTA domain. We find that Cdk phosphorylation of M18BP1 is necessary for M18BP1 to bind CENP-C and localize to centromeres in metaphase. Surprisingly, mutations which disrupt the metaphase M18BP1/CENP-C interaction cause defective nuclear localization of M18BP1 in interphase, resulting in defective CENP-A nucleosome assembly. We propose that M18BP1 may identify centromeric sites in metaphase for subsequent CENP-A nucleosome assembly in interphase.〈/p〉
    Print ISSN: 0261-4189
    Electronic ISSN: 1460-2075
    Topics: Biology , Medicine
    Published by Springer Nature on behalf of The European Molecular Biology Organization (EMBO).
    Location Call Number Expected Availability
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    PAPER CURRENT
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