Cooperation of proto-signals for nuclear accumulation of estrogen and progesterone receptors.

摘要: Abstract Multiple proto-signals (p-NLSs) for nuclear targeting, none of which suffices on its own, cooperate in the estrogen (ER) and progesterone (PR) receptors. In ER, an estrogen-inducible p-NLS was found hormone binding domain (HBD), addition to three lysine/arginine-rich motifs resembling prototype constitutive localization signals (NLSs). The inducible ER p-NLSs presence hydroxy-tamoxifen, but not ICI 164,384. PR, p-NLSs, two are located within directly adjacent second zinc finger, with each other a weak hormone-inducible PR HBD. No 'masking' by HBD observed while ligand-free glucocorticoid receptor inhibited activity both homologous heterologous NLSs. Nuclear co-translocation experiments indicated that vivo stability dimers is hormonally controlled, that, absence cognate ligand, more stable than dimers. This likely account differential requirement DNA vitro.