PHOSDUCIN INHIBITS RECEPTOR PHOSPHORYLATION BY THE BETA-ADRENERGIC-RECEPTOR KINASE IN A PKA-REGULATED MANNER

被引：46

作者：

HEKMAN, M ^{[1
]}

BAUER, PH ^{[1
]}

SOHLEMANN, P ^{[1
]}

LOHSE, MJ ^{[1
]}

机构：

[1] UNIV MUNICH,MAX PLANCK INST BIOCHEM,MOLEC BIOL LAB,D-82152 MARTINSRIED,GERMANY

来源：

FEBS LETTERS | 1994年 / 343卷 / 02期

关键词：

BETA-ADRENERGIC RECEPTOR; BETA-ADRENERGIC RECEPTOR KINASE; PHOSDUCIN; G-PROTEIN;

D O I：

10.1016/0014-5793(94)80302-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Homologous or receptor-specific desensitization of beta-adrenergic receptors is thought to be triggered by receptor phosphorylation mediated by the beta-adrenergic receptor kinases (beta ARK). Upon receptor activation, cytosolic BARK translocates to the membrane, probably by binding to G-protein beta gamma-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 beta ARK for the G-protein beta gamma-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 beta-adrenergic receptor desensitization.

引用

页码：120 / 124

页数：5

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