Molecular basis of the regulation of the lutropin/choriogonadotropin receptor

The studies summarized here clearly show that the phosphorylation of one or more serine residues (S635, S639, S649 and/or S652) present in the C-terminal tail of the LHR is necessary, but not sufficient, for the agonist-induced uncoupling of the LHR from adenylate cyclase and for the endocytosis of...

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Bibliographic Details
Published inBiochemical Society transactions Vol. 25; no. 3; p. 1021
Main Author Ascoli, M
Format Journal Article
LanguageEnglish
Published England 01.08.1997
Subjects
Adenylyl Cyclases - metabolism
Animals
Chorionic Gonadotropin - pharmacology
Down-Regulation
Female
Humans
Leydig Cell Tumor - physiopathology
Leydig Cells - physiology
Male
Models, Molecular
Protein Conformation
Receptors, LH - biosynthesis
Receptors, LH - chemistry
Receptors, LH - physiology
Serine
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Summary:The studies summarized here clearly show that the phosphorylation of one or more serine residues (S635, S639, S649 and/or S652) present in the C-terminal tail of the LHR is necessary, but not sufficient, for the agonist-induced uncoupling of the LHR from adenylate cyclase and for the endocytosis of the agonist-receptor complex. Simultaneous mutation of these four serines to alanines decreases the rate of agonist-induced uncoupling and the rate of agonist-induced internalization. This mutation does not affect the magnitude of agonist-induced uncoupling attained upon a long incubation with agonist, nor does it reduce the rate of internalization of the agonist-bound LHR to that of the free LHR. Thus additional molecular interactions and/or post-translational modifications of the LHR are needed for uncoupling and down-regulation.
ISSN:0300-5127
DOI:10.1042/bst0251021