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The strong hydrophobic domain of the activated estrogen receptor of porcine uterus
Author(s) -
Murayama Akira,
Fukai Fumio
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80590-0
Subject(s) - vero cell , cytoplasm , proteolysis , estrogen receptor , chemistry , binding site , protease , binding domain , receptor , biophysics , microbiology and biotechnology , biology , biochemistry , enzyme , in vitro , cancer , breast cancer , genetics
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.