G contains an unidentified covalent modification that increases its affinity for adenylyl cyclase

C. Kleuss, A. G. Gilman

Research output: Contribution to journalArticle

41 Scopus citations

Abstract

Many G protein α subunits are dually acylated with myristate and palmitate or are palmitoylated on more than one cysteine residue near their N termini. The Gα protein that activates adenylyl cyclase, αs, is not myristoylated but can be reversibly palmitoylated. It appears that αs contains another, as-yet-unidentified covalent modification that decreases its apparent dissociation constant for adenylyl cyclase from 50 nM to <0.5 nM. This modification is at or near the N terminus of the protein and is hydrophobic. Palmitoylation of native αs does not account for its high affinity for adenylyl cyclase.

Original languageEnglish (US)
Pages (from-to)6116-6120
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number12
DOIs
StatePublished - Jun 10 1997

    Fingerprint

ASJC Scopus subject areas

  • General

Cite this