Receptor and effector interactions of Gs Functional studies with antibodies to the αs carboxyl-terminal decapeptide

William F. Simonds, Paul K. Goldsmith, Charles J. Woodard, Cecilia G. Unson, Allen M. Spiegel

Research output: Contribution to journalArticle

147 Scopus citations

Abstract

Antibodies generated to a synthetic decapeptide, RMHLRQYELL, representing the carboxyl-terminus of Gs-α have been characterized in immunoblots and functional studies. This antibody, designated RM, reacts exclusively with a doublet of proteins of 52 and 45 kDa in immunoblots of bovine brain and wild-type S49 murine lymphoma cell membranes. No such reactivity is seen in membranes from cyc- S49 cells, which lack Gs. RM blocks receptor-mediated activation of Gs and adenylyl cyclase in membranes from wild-type S49 cells. RM could also immunoprecipitate adenylyl cyclase activity in detergent extracts from GTP[γ]S- or fluoride-preactivated bovine brain membranes; thus binding of αs to effector and carboxyl-terminal antibody was mutually compatible. Such experiments provide an approach for the elucidation of functionally relevant interactions of G-proteins with receptors and electors in the membrane.

Original languageEnglish (US)
Pages (from-to)189-194
Number of pages6
JournalFEBS Letters
Volume249
Issue number2
DOIs
StatePublished - Jun 5 1989
Externally publishedYes

Keywords

  • Adenylyl cyclase
  • Adrenergic receptor, β-
  • GTP-binding protein
  • Immunoprecipitation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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