An Asp79Asn mutation of the α2A‐adrenoceptor interferes equally with agonist activation of individual Giα‐family G protein subtypes

FEBS Letters

Ward, Richard J¹  Milligan, Graeme¹ 

[1] Molecular Pharmacology Group, Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, Davidson Building, University of Glasgow, Glasgow G12 8QQ, UK

关键词: G protein-coupled receptor;    G protein;    Adrenaline;    GTPase;    GPCR;    G protein-coupled receptor;   

DOI  :  10.1016/S0014-5793(99)01581-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The quantitative effects of an Asp⁷⁹Asn mutation in the porcine α_2A-adrenoceptor on adrenaline-mediated stimulation of the α subunit of individual members of the G_i family of G proteins were assessed by measuring GTP turnover number for fusion proteins between the wild type or mutated receptor and pertussis toxin-resistant forms of each of G_i1, G_i2 and G_i3. In each case the receptor mutation limited activation of the G protein to 8–14% of that produced by the wild type receptor. Previous demonstration that in a single cell this mutation selectively interferes with α_2A-adrenoceptor regulation of distinct effector end points transduced by G_i family members must therefore reflect differential requirements for amplification or the cellular location of individual, co-expressed, G proteins.

【 授权许可】

Unknown