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Phosducin inhibits receptor phosphorylation by the β‐adrenergic receptor kinase in a PKA‐regulated manner
Author(s) -
Hekman Mirko,
Bauer Petra H.,
Söhlemann Peter,
Lohse Martin J.
Publication year - 1994
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(94)80302-1
Subject(s) - phosphorylation , microbiology and biotechnology , chemistry , protein kinase a , receptor , biochemistry , biology
Homologous or receptor‐specific desensitization of β‐adrenergic receptors is thought to be triggered by receptor phosphorylation mediated by the β‐adrenergic receptor kinases (ßARK). Upon receptor activation, cytosolic ßARK translocates to the membrane, probably by binding to G‐protein βγ‐subunits. Using the purified proteins reconstituted into phospholipid vesicles we show here that this binding process can be inhibited by phosducin, a cytosolic protein that has recently been described as a regulator of G‐protein‐mediated signalling. Phosducin appears to complete very effectively with ßARK for the G‐protein βγ‐subunits. These inhibitory effects of phosducin on receptor phosphorylation are antagonized following phosphorylation of phosducin by protein kinase A. It is proposed that phosducin may act as a regulator of homologous β‐adrenergic receptor desensitization.