Abstract
The retinoblastoma protein (pRb) is a master regulator of the cell cycle, cell differentiation and apoptosis 1 Herwig S. Strauss M. The retinoblastoma protein: a master regulator of cell cycle, differentiation and apoptosis. Eur. J. Biochem. 1997; 246: 581-601 Crossref PubMed Scopus (217) Google Scholar . In humans, pRb and its related proteins, p107 and p130, are potent inhibitors of gene transcription mediated by the E2F family of transcription factors 2 Dyson N. The regulation of E2F by pRB-family proteins. Genes Dev. 1998; 12: 2245-2262 Crossref PubMed Scopus (1955) Google Scholar . Interaction of pRb with E2F results in the formation of a transcription–repressive complex that constrains expression of E2F-target genes and, consequently, the progression of cells into S phase. The pRb–E2F repressive complex can act by sequestering transcription activators, or by recruiting histone deacetylases 3 Brehm A. Kouzarides T. Retinoblastoma protein meets chromatin. Trends Biochem. Sci. 1999; 24: 142-145 Abstract Full Text Full Text PDF PubMed Scopus (125) Google Scholar or repressor proteins 4 Meloni A.R. et al. A mechanism for Rb/p130-mediated transcriptional repression involving recruitment of the CtBP corepressor. Proc. Natl. Acad. Sci. U. S. A. 1999; 96: 9574-9579 Crossref PubMed Scopus (165) Google Scholar . Here we present data that suggests the operation of a novel transcriptional repression mechanism involving the interaction of pRb with heterochromatin-associated proteins.
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