Murayama A, Fukai F
FEBS Lett. 1983 Jul 25;158(2):255-8. doi: 10.1016/0014-5793(83)80590-0.
Basic estrogen receptor (ER) molecule (vero-ER) of porcine uterus, which was previously shown to be the activated ER necessary to translocate from the cytoplasm into the nucleus, possesses a strongly hydrophobic nature. The strong hydrophobicity of vero-ER was concealed through binding with ER-binding factors (ERBFs). Vero-ER lost its strong hydrophobicity and its capability to bind with ERBFs after limited proteolysis by endogenous protease. The strong hydrophobic domain of vero-ER, indispensable for the nuclear translocation, was assumed to be located near the binding site with ERBFs.
猪子宫的基本雌激素受体(ER)分子(vero-ER),先前被证明是从细胞质转运到细胞核所必需的活化ER,具有很强的疏水性。vero-ER的强疏水性通过与雌激素受体结合因子(ERBFs)结合而被掩盖。经内源性蛋白酶有限酶解后,vero-ER失去了其强疏水性及其与ERBFs结合的能力。vero-ER的强疏水域对于核转位是不可或缺的,据推测它位于与ERBFs的结合位点附近。