| Literature DB >> 10706618 |
C Abbondanza1, N Medici, V Nigro, V Rossi, L Gallo, G Piluso, A Belsito, A Roscigno, P Bontempo, A A Puca, A M Molinari, B Moncharmont, G A Puca.
Abstract
Co-immunoprecipitation experiments in cell extract from cultured cells or target tissues indicated that estrogen receptor was complexed with the retinoblastoma binding protein RIZ in a ligand-dependent manner. Mapping of interaction sites indicated that in both proteins the same regions and motifs responsible for the interaction of transcriptional co-activator and nuclear receptors were involved. In cultured cells, estradiol induced a redistribution of RIZ protein within the nucleus and in the cytoplasm. A similar effect was produced in vivo, in prepuberal rat endometrium, by administration of a physiological dose of estradiol. Therefore, RIZ protein could be a specific effector of estrogen action downstream of the hormone-receptor interaction, presumably involved in proliferation control.Entities:
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Year: 2000 PMID: 10706618 PMCID: PMC16204 DOI: 10.1073/pnas.97.7.3130
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205