Phosducin inhibits receptor phosphorylation by the β‐adrenergic receptor kinase in a PKA‐regulated manner

FEBS Letters

Söhlemann, Peter¹  Hekman, Mirko¹  Lohse, Martin J.¹  Bauer, Petra H.¹ 

[1] Laboratory of Molecular Biology, University of Munich, Max-Planck-Institute of Biochemistry, 82152 Martinsried, Germany

关键词: β-Adrenergic receptor;    β-Adrenergic receptor kinase;    Phosducin;    G-protein;    ßARK;    β-adrenergic receptor kinase;    PKA;    protein kinase A;    PKI;    inhibitor of protein kinase A;   

DOI  :  10.1016/0014-5793(94)80302-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown