Identification of a Gs-protein coupling domain to the β-aderenoceptor using site-specific synthetic peptides. Carboxyl terminus of Gsα is involved in coupling to β-adrenoceptors

Dieter Palm; Gerald Münch; Daria Malek; Christian Dees; Mirko Hekman

doi:10.1016/0014-5793(90)80575-4

Identification of a G_s-protein coupling domain to the β-aderenoceptor using site-specific synthetic peptides. Carboxyl terminus of G_sα is involved in coupling to β-adrenoceptors

Dieter Palm
, Gerald Münch
, Daria Malek
, Christian Dees
, Mirko Hekman

University of Würzburg

Research output: Contribution to journal › Article › peer-review

53 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	294-298
Number of pages	5
Journal	FEBS Letters
Volume	261
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(90)80575-4
Publication status	Published - 26 Feb 1990
Externally published	Yes

Keywords

Adrenoceptor, β-, G-protein
Anti-peptide antibody
Coupling domain
Synthetic peptide

Access to Document

10.1016/0014-5793(90)80575-4

Cite this

@article{fa94f6c77490430ab3c167db949f92ea,

title = "Identification of a Gs-protein coupling domain to the β-aderenoceptor using site-specific synthetic peptides. Carboxyl terminus of Gsα is involved in coupling to β-adrenoceptors",

abstract = "Competition between Gs-protein and the synthetic peptide, GSA 379-394, derived from the carboxyl-terminal region of the αs-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 αt-,αil- or αo-subunits did not interfere with β-receptor-Gs coupling. The direct coupling between Gs 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.",

keywords = "Adrenoceptor, β-, G-protein, Anti-peptide antibody, Coupling domain, Synthetic peptide",

author = "Dieter Palm and Gerald M{\"u}nch and Daria Malek and Christian Dees and Mirko Hekman",

year = "1990",

month = feb,

day = "26",

doi = "10.1016/0014-5793(90)80575-4",

language = "English",

volume = "261",

pages = "294--298",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc",

number = "2",

}

TY - JOUR

T1 - Identification of a Gs-protein coupling domain to the β-aderenoceptor using site-specific synthetic peptides. Carboxyl terminus of Gsα is involved in coupling to β-adrenoceptors

AU - Palm, Dieter

AU - Münch, Gerald

AU - Malek, Daria

AU - Dees, Christian

AU - Hekman, Mirko

PY - 1990/2/26

Y1 - 1990/2/26

N2 - Competition between Gs-protein and the synthetic peptide, GSA 379-394, derived from the carboxyl-terminal region of the αs-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 αt-,αil- or αo-subunits did not interfere with β-receptor-Gs coupling. The direct coupling between Gs 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.

AB - Competition between Gs-protein and the synthetic peptide, GSA 379-394, derived from the carboxyl-terminal region of the αs-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 αt-,αil- or αo-subunits did not interfere with β-receptor-Gs coupling. The direct coupling between Gs 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.

KW - Adrenoceptor, β-, G-protein

KW - Anti-peptide antibody

KW - Coupling domain

KW - Synthetic peptide

UR - https://www.scopus.com/pages/publications/0025193724

U2 - 10.1016/0014-5793(90)80575-4

DO - 10.1016/0014-5793(90)80575-4

M3 - Article

C2 - 2155823

AN - SCOPUS:0025193724

SN - 0014-5793

VL - 261

SP - 294

EP - 298

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

Identification of a G_s-protein coupling domain to the β-aderenoceptor using site-specific synthetic peptides. Carboxyl terminus of G_sα is involved in coupling to β-adrenoceptors

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this