Identification of a Gs‐protein coupling domain to the β‐aderenoceptor using site‐specific synthetic peptides

FEBS Letters

Palm, Dieter¹  Malek, Daria¹  Dees, Christian¹  Münch, Gerald¹  Hekman, Mirko¹ 

[1] Department of Physiological Chemistry, University of Würzburg, Koellikerstraße 2, D-8700 Würzburg, FRG

关键词: Adrenoceptor;    β-;    Gs-protein;    Coupling domain;    Synthetic peptide;    Anti-peptide antibody;    Gs-protein;    guanine nucleotide-binding protein mediating stimulation of adenylate cyclase;    αt;    αo and αil;    α-subunits of corresponding G-proteins;    C;    adenylate cyclase;    GTPγS;    guanosine-5'-O-(3-thiotriphosphate);    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/0014-5793(90)80575-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Competition between G_s-protein and the synthetic peptide, GSA 379-394, derived from the carboxyl-terminal region of the α_s-subunit, led to complete inhibition of receptor-mediated adenylate cyclase activation in turkey erythrocyte membranes. Related peptides corresponding to the homologous carboxyl-terminal region of α_t-,α_il- or α_o-subunits did not interfere with β-receptor-G_s coupling. The direct coupling between G_s and adenylate cyclase was not influenced by any of these peptides. These results emphasize the important role of the carboxyl-terminus of G-protein α-subunits for the specific recognition of their corresponding receptors and for signal transduction.

【 授权许可】

Unknown