Abstract:
:Phorbol-esters have been shown to modulate the beta-adrenergic-stimulated adenylyl cyclase in a number of cell lines. Here, using site directed mutagenesis, we investigate the role of the beta 2-adrenergic receptor phosphorylation by protein kinase C in this regulatory process. Mutation of the serine-261, -262, -344 and -345 of the beta 2-adrenergic receptor prevented the phorbol-ester-induced phosphorylation of the receptor. This mutation also abolished the phorbol-ester-induced decrease in high-affinity agonist binding and potency of the beta 2-adrenergic receptor. We suggest that protein kinase C mediated phosphorylation of the receptor promotes its functional uncoupling.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Bouvier M,Guilbault N,Bonin Hdoi
10.1016/0014-5793(91)80159-zsubject
Has Abstractpub_date
1991-02-25 00:00:00pages
243-8issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(91)80159-Zjournal_volume
279pub_type
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