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β-肾上腺素能受体激酶2对G蛋白βγ亚基的选择性。

Selectivity of beta-adrenergic receptor kinase 2 for G protein betagamma subunits.

作者信息

Müller S, Straub A, Lohse M J

机构信息

Institute of Pharmacology, University of Würzburg, Germany.

出版信息

FEBS Lett. 1997 Jan 13;401(1):25-9. doi: 10.1016/s0014-5793(96)01424-x.

Abstract

Phosphorylation of G protein-coupled receptors by beta-adrenergic receptor kinases (betaARK) requires the presence of G protein betagamma subunits. We have investigated the ability of the two betaARK isoforms to distinguish between defined recombinant betagamma subunits. betaARK2 had an about 25% lower specific activity than betaARK1 towards rhodopsin and the beta2-adrenergic receptor but the two kinases shared the selectivity for betagamma subunits: betagamma complexes consisting of beta1 or beta2 in combination with gamma2, gamma5, and gamma7 were more efficacious than those with gamma3 or beta1 gamma1. Thus, while betaARKs differentiate between defined betagamma subunits, betagamma complexes do not discriminate between betaARK isoforms.

摘要

β - 肾上腺素能受体激酶(βARK)对G蛋白偶联受体的磷酸化作用需要G蛋白βγ亚基的存在。我们研究了两种βARK同工型区分特定重组βγ亚基的能力。βARK2对视紫红质和β2 - 肾上腺素能受体的比活性比βARK1低约25%,但这两种激酶对βγ亚基具有相同的选择性:由β1或β2与γ2、γ5和γ7组合而成的βγ复合物比与γ3或β1γ1组合的复合物更有效。因此,虽然βARKs能区分特定的βγ亚基,但βγ复合物不能区分βARK同工型。

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