期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 110, 期 21, 页码 8579-8584出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1302955110
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资金
- Institut National de la Sante et de la Recherche Medicale
- Centre National de la Recherche Scientifique
- Institut National du Cancer [INCa_4496, INCa_4454]
- Agence Nationale de la Recherche (VariZome) [ANR-12-BSV8-0018-01]
- Agence Nationale de la Recherche (Nucleoplat) [NT09_476241]
- Agence Nationale de la Recherche (CHROME) [ANR-12-BSV5-0017-03 Blanc SVSE 5]
- Association pour la Recherche sur le Cancer [ARC SFI20101201822]
- Agence Nationale de la Recherche (ANR) [ANR-12-BSV8-0018] Funding Source: Agence Nationale de la Recherche (ANR)
The role of the mitotic phosphorylation of the amino (NH2) terminus of Centromere Protein A (CENP-A), the histone variant epigenetic centromeric marker, remains elusive. Here, we show that the NH2 terminus of human CENP-A is essential for mitotic progression and that localization of CENP-C, another key centromeric protein, requires only phosphorylation of the CENP-A NH2 terminus, and is independent of the CENP-A NH2 terminus length and amino acid sequence. Mitotic CENP-A nucleosomal complexes contain CENP-C and phospho-binding 14-3-3 proteins. In contrast, mitotic nucleosomal complexes carrying nonphosphorylatable CENP-A-S7A contained only low levels of CENP-C and no detectable 14-3-3 proteins. Direct interactions between the phosphorylated form of CENP-A and 14-3-3 proteins as well as between 14-3-3 proteins and CENP-C were demonstrated. Taken together, our results reveal that 14-3-3 proteins could act as specific mitotic bridges, linking phosphorylated CENP-A and CENP-C, which are necessary for the platform function of CENP-A centromeric chromatin in the assembly and maintenance of active kinetochores.
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