A region of adenylyl cyclase 2 critical for regulation by G protein βγ subunits

Jianqiang Chen, Michael DeVivo, Jane Dingus, Anya Harry, Jingrong Li, Jinliang Sui, Donna J. Carty, Jonathan L. Blank, John H. Exton, Robert H. Stoffel, James Inglese, Robert J. Lefkowitz, Diomedes E. Logothetis, John D. Hildebrandt, Ravi Iyengar

Research output: Contribution to journalArticlepeer-review

235 Scopus citations

Abstract

Receptor-mediated activation of heterotrimeric guanine nucleotide-binding proteins (G proteins) results in the dissociation of α from βγ subunits, thereby allowing both to regulate effectors. Little is known about the regions of effectors required for recognition of Gβγ. A peptide encoding residues 956 to 982 of adenylyl cyclase 2 specifically blocked Gβγ stimulation of adenylyl cyclase 2, phospholipase C-β3, potassium channels, and β-adrenergic receptor kinase as well as inhibition of calmodulin-stimulated adenylyl cyclases, but had no effect on interactions between Gβγ and Gαo. Substitutions in this peptide identified a functionally important motif, Gln-X-X-Glu-Arg, that is also conserved in regions of potassium channels and β-adrenergic receptor kinases that participate in Gβγ interactions. Thus, the region defined by residues 956 to 982 of adenylyl cyclase 2 may contain determinants important for receiving signals from Gβγ.

Original languageEnglish
Pages (from-to)1166-1169
Number of pages4
JournalScience
Volume268
Issue number5214
DOIs
StatePublished - 1995
Externally publishedYes

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