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Gene Review

RBBP4  -  retinoblastoma binding protein 4

Homo sapiens

Synonyms: CAF-1 subunit C, CAF-I 48 kDa subunit, CAF-I p48, Chromatin assembly factor 1 subunit C, Chromatin assembly factor I p48 subunit, ...
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Disease relevance of RBBP4


High impact information on RBBP4

  • RNAi knockdown in human cells shows that Mis16 function is conserved as RbAp48 and RbAp46 are both required for localization of human CENP-A [3].
  • In mammals, Rb and related proteins act as regulators of E2F transcription factors, and RbAp48 may act with such proteins as a transcriptional corepressor [4].
  • The human SAP30 complex is active in deacetylating core histone octamers, but inactive in deacetylating nucleosomal histones due to the inability of the histone binding proteins RbAp46 and RbAp48 to gain access to nucleosomal histones [5].
  • Two closely related mammalian RB binding proteins, RbAp48 and RbAp46, share sequence homology with the Msi1 protein of yeast [6].
  • Human RbAp48 is present in protein complexes involved in histone acetylation and chromatin assembly [6].

Biological context of RBBP4


Anatomical context of RBBP4

  • Indeed, transgenic expression of the RbAp48 gene induced apoptosis in the exocrine glands but not in other organs [7].
  • Exogenous RPD3 may be targeted to histones through interaction with endogenous RbAp48 to direct transcriptional repression of the Xenopus TRbetaA promoter in the oocyte nucleus [10].
  • To biologically validate our classifier, we transfected RbAp48 into three cancer cell lines (HS-578T, MALME-3M, and MDA-MB-231) [11].
  • To examine the Jurkat cell interaction partners of RbAp48, we digested entire immunoaffinity extracts with trypsin and identified potential interacting proteins using one- and two-dimensional microcapillary HPLC-ion-trap mass spectrometry [12].

Associations of RBBP4 with chemical compounds


Other interactions of RBBP4

  • A subset of these mutations also cause a decreased interaction with the HDAC1-associated proteins RbAp48 and mSin3A [13].
  • A multiprotein complex is recruited to the hLHR promoter via interaction with Sp1/Sp3: HDACs dock directly to Sp1-1 bound DNA and indirectly to Sp3-1 bound DNA through RbAp48, while mSin3A interacts HDACs and potentiates HDAC1-mediated repression [14].
  • Here we report that BRCA1 interacts in vivo and in vitro with the Rb-binding proteins, RbAp46 and RbAp48, as well as with Rb [15].
  • CTIP2 was found to associate with the NuRD complex through direct interaction with both RbAp46 and RbAp48, and components of the NuRD complex were found to be recruited to an artificial promoter template in a CTIP2-dependent manner in transfected cells [16].
  • The genes encoding Beclin 1, RbAp48, Pir51 and aldolase b are first reported that may be related with hepatocarcinoma [17].

Analytical, diagnostic and therapeutic context of RBBP4


  1. RbAp48 belongs to the histone deacetylase complex that associates with the retinoblastoma protein. Nicolas, E., Morales, V., Magnaghi-Jaulin, L., Harel-Bellan, A., Richard-Foy, H., Trouche, D. J. Biol. Chem. (2000) [Pubmed]
  2. RbAp48 is a target of nuclear factor-kappaB activity in thyroid cancer. Pacifico, F., Paolillo, M., Chiappetta, G., Crescenzi, E., Arena, S., Scaloni, A., Monaco, M., Vascotto, C., Tell, G., Formisano, S., Leonardi, A. J. Clin. Endocrinol. Metab. (2007) [Pubmed]
  3. 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]
  4. lin-35 and lin-53, two genes that antagonize a C. elegans Ras pathway, encode proteins similar to Rb and its binding protein RbAp48. Lu, X., Horvitz, H.R. Cell (1998) [Pubmed]
  5. SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex. Zhang, Y., Sun, Z.W., Iratni, R., Erdjument-Bromage, H., Tempst, P., Hampsey, M., Reinberg, D. Mol. Cell (1998) [Pubmed]
  6. A conserved family of WD-40 proteins binds to the retinoblastoma protein in both plants and animals. Ach, R.A., Taranto, P., Gruissem, W. Plant Cell (1997) [Pubmed]
  7. Novel role for RbAp48 in tissue-specific, estrogen deficiency-dependent apoptosis in the exocrine glands. Ishimaru, N., Arakaki, R., Omotehara, F., Yamada, K., Mishima, K., Saito, I., Hayashi, Y. Mol. Cell. Biol. (2006) [Pubmed]
  8. Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB. Zhang, Q., Vo, N., Goodman, R.H. Mol. Cell. Biol. (2000) [Pubmed]
  9. Dual retinoblastoma-binding proteins with properties related to a negative regulator of ras in yeast. Qian, Y.W., Lee, E.Y. J. Biol. Chem. (1995) [Pubmed]
  10. Functional analysis of the SIN3-histone deacetylase RPD3-RbAp48-histone H4 connection in the Xenopus oocyte. Vermaak, D., Wade, P.A., Jones, P.L., Shi, Y.B., Wolffe, A.P. Mol. Cell. Biol. (1999) [Pubmed]
  11. Prediction of radiation sensitivity using a gene expression classifier. Torres-Roca, J.F., Eschrich, S., Zhao, H., Bloom, G., Sung, J., McCarthy, S., Cantor, A.B., Scuto, A., Li, C., Zhang, S., Jove, R., Yeatman, T. Cancer Res. (2005) [Pubmed]
  12. Use of MEDUSA-based data analysis and capillary HPLC-ion-trap mass spectrometry to examine complex immunoaffinity extracts of RBAp48. Gururaja, T., Li, W., Bernstein, J., Payan, D.G., Anderson, D.C. J. Proteome Res. (2002) [Pubmed]
  13. A role for histone deacetylase activity in HDAC1-mediated transcriptional repression. Hassig, C.A., Tong, J.K., Fleischer, T.C., Owa, T., Grable, P.G., Ayer, D.E., Schreiber, S.L. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  14. Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes. Zhang, Y., Dufau, M.L. J. Steroid Biochem. Mol. Biol. (2003) [Pubmed]
  15. BRCA1 interacts with components of the histone deacetylase complex. Yarden, R.I., Brody, L.C. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  16. CTIP2 Associates with the NuRD Complex on the Promoter of p57KIP2, a Newly Identified CTIP2 Target Gene. Topark-Ngarm, A., Golonzhka, O., Peterson, V.J., Barrett, B., Martinez, B., Crofoot, K., Filtz, T.M., Leid, M. J. Biol. Chem. (2006) [Pubmed]
  17. Genes encoding Pir51, Beclin 1, RbAp48 and aldolase b are up or down-regulated in human primary hepatocellular carcinoma. Song, H., Xia, S.L., Liao, C., Li, Y.L., Wang, Y.F., Li, T.P., Zhao, M.J. World J. Gastroenterol. (2004) [Pubmed]
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