Selectivity of β‐adrenergic receptor kinase 2 for G protein βγ subunits

FEBS Letters

Müller, Stefan¹  Lohse, Martin J¹  Straub, Annette¹ 

[1] Institute of Pharmacology, University of Würzburg, Versbacher Str. 9, 97078 Würzburg, Germany

关键词: β-Adrenergic receptor kinase;    β2-Adrenergic receptor;    Rhodopsin;    G protein βγ subunit;    βARK;    β-adrenergic receptor kinase;    β2AR;    β2-adrenergic receptor;    βγB;    bovine brain-βγ;    βγT;    transducin-βγ;    GRK;    G protein-coupled receptor kinase;   

DOI  :  10.1016/S0014-5793(96)01424-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phosphorylation of G protein-coupled receptors by β-adrenergic receptor kinases (βARK) requires the presence of G protein βγ subunits. We have investigated the ability of the two βARK isoforms to distinguish between defined recombinant βγ subunits. βARK2 had an about 25% lower specific activity than βARK1 towards rhodopsin and the β₂-adrenergic receptor but the two kinases shared the selectivity for βγ subunits: βγ complexes consisting of β₁ or β₂ in combination with γ₂, γ₅, and γ₇ were more efficacious than those with γ₃ or β₁γ₁. Thus, while βARKs differentiate between defined βγ subunits, βγ complexes do not discriminate between βARK isoforms.

【 授权许可】

Unknown