Structure, Dynamics, and Cloning of the Estrogen Receptor

Abstract

Recent biochemical (Welshons et al., 1984) and immunocytochemical data (King and Greene, 1984; Press and Greene, 1984; Press et al., 1985) suggest that the majority of functional estrogen receptor may reside in the nucleus, regardless of hormone status, and that binding of hormone to receptor leads to a tighter association of steroid-receptor complex with nuclear components. The nature of this association is not known, although a number of nuclear acceptor sites have been proposed, including specific DNA sequences (Cato et al., 1984; Jost et al., 1985; Compton et al., 1983; Payvar et al., 1983), ribonucleoprotein (Liang and Liao, 1974), basic nonhistone proteins (Puca et al., 1974), the nuclear matrix (Barrack and Coffey, 1980; Barrack, 1983) and acidic nonhistone protein/DNA complexes (Spelsberg et al., 1983). The biological significance of these results has not been established, and, as yet, no one has been able to reconstitute all of the cellular components required for steroid hormone response in any cell-free system.