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Identification of a G s ‐protein coupling domain to the β‐aderenoceptor using site‐specific synthetic peptides
Author(s) -
Palm Dieter,
Münch Gerald,
Malek Daria,
Dees Christian,
Hekman Mirko
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80575-4
Subject(s) - adenylate kinase , cyclase , protein subunit , receptor , peptide , g protein , g protein coupled receptor , chemistry , biochemistry , signal transduction , coupling (piping) , biology , gene , mechanical engineering , engineering
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.