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Gene Review

CENPA  -  centromere protein A

Homo sapiens

Synonyms: CENP-A, CenH3, Centromere autoantigen A, Centromere protein A, Histone H3-like centromeric protein A
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Disease relevance of CENPA


High impact information on CENPA

  • Mis16 and Mis18 are required for CENP-A loading and histone deacetylation at centromeres [6].
  • RNAi knockdown in human cells shows that Mis16 function is conserved as RbAp48 and RbAp46 are both required for localization of human CENP-A [6].
  • Many of these proteins, such as the centromeric histone variant CENP-A, and entire subcomplexes, such as the Ndc80(Hec1) complex, are conserved from yeast to humans despite the diverse nature of the DNA sequences on which they assemble [7].
  • We now show in human cells and in yeast that depletion of CENP-A is lethal, but recruitment of normal levels of kinetochore proteins, centromere-generated mitotic checkpoint signaling, chromosome segregation, and viability can be rescued by histone H3 carrying the CATD [8].
  • The CENP-A NAC is essential, as disruption of the complex causes errors of chromosome alignment and segregation that preclude cell survival despite continued centromere-derived mitotic checkpoint signalling [9].

Biological context of CENPA


Anatomical context of CENPA


Associations of CENPA with chemical compounds

  • However, long-term culture in selective medium, or short-term treatment with the histone deacetylase inhibitor Trichostatin A (TSA), promoted the re-assembly of CENPA, -B and -C at the YAC site and the release of minichromosomes containing the YAC integration site [16].
  • Mammalian centromere function depends upon a specialized chromatin organization where distinct domains of CENP-A and dimethyl K4 histone H3, forming centric chromatin, are uniquely positioned on or near the surface of the chromosome [17].
  • Consistent with this finding, depletion of BubR1 increases phosphorylation of CENP-A, a kinetochore-specific Aurora kinase substrate [18].
  • CENP-A and heterochromatin were assembled over noncentromeric DNA, including the gene blasticidin, into nonoverlapping domains [19].
  • Blasticidin transcripts were enriched at sites of CENP-A binding but not at H3 methylated at lysine 9, indicating that formation of CEN chromatin within a repetitive DNA environment does not preclude gene expression [19].
  • Tricostatin A, an inhibitor to histone deacetylase, suppresses the loss of CENP-A recruitment to centromeres in hMis18alpha RNAi cells [20].

Physical interactions of CENPA


Co-localisations of CENPA


Other interactions of CENPA


Analytical, diagnostic and therapeutic context of CENPA


  1. Overexpression and mistargeting of centromere protein-A in human primary colorectal cancer. Tomonaga, T., Matsushita, K., Yamaguchi, S., Oohashi, T., Shimada, H., Ochiai, T., Yoda, K., Nomura, F. Cancer Res. (2003) [Pubmed]
  2. A novel centromere monospecific serum to a human autoepitope on the histone H3-like protein CENP-A. Valdivia, M.M., Figueroa, J., Iglesias, C., Ortíz, M. FEBS Lett. (1998) [Pubmed]
  3. Development of a CENP-A/CENP-B-specific immune response in a patient with systemic sclerosis. Mahler, M., Mierau, R., Genth, E., Blüthner, M. Arthritis Rheum. (2002) [Pubmed]
  4. Molecular cloning and sequence analysis of hamster CENP-A cDNA. Figueroa, J., Pendón, C., Valdivia, M.M. BMC Genomics (2002) [Pubmed]
  5. Detection of anticentromere antibodies using recombinant human CENP-A protein. Sun, D., Martinez, A., Sullivan, K.F., Sharp, G.C., Hoch, S.O. Arthritis Rheum. (1996) [Pubmed]
  6. Mis16 and Mis18 are required for CENP-A loading and histone deacetylation at centromeres. Hayashi, T., Fujita, Y., Iwasaki, O., Adachi, Y., Takahashi, K., Yanagida, M. Cell (2004) [Pubmed]
  7. Kinetochore-spindle microtubule interactions during mitosis. Kline-Smith, S.L., Sandall, S., Desai, A. Curr. Opin. Cell Biol. (2005) [Pubmed]
  8. Centromere identity maintained by nucleosomes assembled with histone H3 containing the CENP-A targeting domain. Black, B.E., Jansen, L.E., Maddox, P.S., Foltz, D.R., Desai, A.B., Shah, J.V., Cleveland, D.W. Mol. Cell (2007) [Pubmed]
  9. The human CENP-A centromeric nucleosome-associated complex. Foltz, D.R., Jansen, L.E., Black, B.E., Bailey, A.O., Yates, J.R., Cleveland, D.W. Nat. Cell Biol. (2006) [Pubmed]
  10. CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role in completion of cytokinesis. Zeitlin, S.G., Shelby, R.D., Sullivan, K.F. J. Cell Biol. (2001) [Pubmed]
  11. Mapping the assembly pathways that specify formation of the trilaminar kinetochore plates in human cells. Liu, S.T., Rattner, J.B., Jablonski, S.A., Yen, T.J. J. Cell Biol. (2006) [Pubmed]
  12. CENP-A phosphorylation by Aurora-A in prophase is required for enrichment of Aurora-B at inner centromeres and for kinetochore function. Kunitoku, N., Sasayama, T., Marumoto, T., Zhang, D., Honda, S., Kobayashi, O., Hatakeyama, K., Ushio, Y., Saya, H., Hirota, T. Dev. Cell (2003) [Pubmed]
  13. CENP-G: a new centromeric protein that is associated with the alpha-1 satellite DNA subfamily. He, D., Zeng, C., Woods, K., Zhong, L., Turner, D., Busch, R.K., Brinkley, B.R., Busch, H. Chromosoma (1998) [Pubmed]
  14. Centromere/kinetochore localization of human centromere protein A (CENP-A) exogenously expressed as a fusion to green fluorescent protein. Sugimoto, K., Fukuda, R., Himeno, M. Cell Struct. Funct. (2000) [Pubmed]
  15. Relevance of histone acetylation and replication timing for deposition of centromeric histone CENP-A. Ouspenski, I.I., Van Hooser, A.A., Brinkley, B.R. Exp. Cell Res. (2003) [Pubmed]
  16. Epigenetic assembly of centromeric chromatin at ectopic alpha-satellite sites on human chromosomes. Nakano, M., Okamoto, Y., Ohzeki, J., Masumoto, H. J. Cell. Sci. (2003) [Pubmed]
  17. H2A.Z contributes to the unique 3D structure of the centromere. Greaves, I.K., Rangasamy, D., Ridgway, P., Tremethick, D.J. Proc. Natl. Acad. Sci. U.S.A. (2007) [Pubmed]
  18. The human mitotic checkpoint protein BubR1 regulates chromosome-spindle attachments. Lampson, M.A., Kapoor, T.M. Nat. Cell Biol. (2005) [Pubmed]
  19. Human centromeric chromatin is a dynamic chromosomal domain that can spread over noncentromeric DNA. Lam, A.L., Boivin, C.D., Bonney, C.F., Rudd, M.K., Sullivan, B.A. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  20. Priming of centromere for CENP-A recruitment by human hMis18alpha, hMis18beta, and M18BP1. Fujita, Y., Hayashi, T., Kiyomitsu, T., Toyoda, Y., Kokubu, A., Obuse, C., Yanagida, M. Dev. Cell (2007) [Pubmed]
  21. CENP-A, -B, and -C chromatin complex that contains the I-type alpha-satellite array constitutes the prekinetochore in HeLa cells. Ando, S., Yang, H., Nozaki, N., Okazaki, T., Yoda, K. Mol. Cell. Biol. (2002) [Pubmed]
  22. The constitutive centromere component CENP-50 is required for recovery from spindle damage. Minoshima, Y., Hori, T., Okada, M., Kimura, H., Haraguchi, T., Hiraoka, Y., Bao, Y.C., Kawashima, T., Kitamura, T., Fukagawa, T. Mol. Cell. Biol. (2005) [Pubmed]
  23. Assembly of additional heterochromatin distinct from centromere-kinetochore chromatin is required for de novo formation of human artificial chromosome. Nakashima, H., Nakano, M., Ohnishi, R., Hiraoka, Y., Kaneda, Y., Sugino, A., Masumoto, H. J. Cell. Sci. (2005) [Pubmed]
  24. Centromere targeting of the chromosomal passenger complex requires a ternary subcomplex of Borealin, Survivin, and the N-terminal domain of INCENP. Klein, U.R., Nigg, E.A., Gruneberg, U. Mol. Biol. Cell (2006) [Pubmed]
  25. Human centromere protein A (CENP-A) can replace histone H3 in nucleosome reconstitution in vitro. Yoda, K., Ando, S., Morishita, S., Houmura, K., Hashimoto, K., Takeyasu, K., Okazaki, T. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  26. Assembly of CENP-A into centromeric chromatin requires a cooperative array of nucleosomal DNA contact sites. Shelby, R.D., Vafa, O., Sullivan, K.F. J. Cell Biol. (1997) [Pubmed]
  27. CENP-B box is required for de novo centromere chromatin assembly on human alphoid DNA. Ohzeki, J., Nakano, M., Okada, T., Masumoto, H. J. Cell Biol. (2002) [Pubmed]
  28. The centromere protein CENP-B behaves as a microtubule-associated protein. Armas-Portela, R., Kremer, L., Avila, J. Acta Histochem. Suppl. (1991) [Pubmed]
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