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
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
收藏
页码:120 / 124
页数:5
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