Biosynthesis and posttranslational finishing of the estradiol receptor.
The time course of subcellular receptor distribution in porcine endometrial epithelium was studied after intrauterine administration of estradiol alone or in combination with puromycin. In untreated cells, the major proportion of receptor is associated with cytoplasmic membranes. The solubilization of receptor from isolated nuclei is independent of their estradiol content. Smooth cytoplasmic membranes are the site of origin of receptor which is swiftly translocated into the nucleus in a 1:1 ratio with the hormone after exposure of the cells to estradiol. Simultaneously administered puromycin delays receptor synthesis and reveals that the nuclear passage of receptor is terminated by receptor degradation. The synthesis of receptor proceeds in rough endoplasmic membranes. A subsequent finishing and deposition in smooth membranes depends on intact protein synthesis.
Sierralta
W D
WD
Max-Planck-Institut für experimentelle Endokrinologie, Hannover, Federal Republic of Germany.
Szendro
P I
PI
Kallweit
E
E
Jungblut
P W
PW
D000818:Animals; D001692:Biological Transport; D003864:Depression, Chemical; D004717:Endometrium / Q000378:metabolism; D004958:Estradiol / Q000494:pharmacology; D005260:Female; D005786:Gene Expression Regulation / Q000187:drug effects; D008861:Microsomes / Q000032:analysis; D014176:Protein Biosynthesis / Q000187:drug effects; D011499:Protein Processing, Post-Translational; D011691:Puromycin / Q000494:pharmacology; D011959:Receptors, Estradiol / Q000096:biosynthesis*; D011960:Receptors, Estrogen / Q000096:biosynthesis*; D013552:Swine
D011959:Receptors, Estradiol; D011960:Receptors, Estrogen; D011691:Puromycin; D004958:Estradiol