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

C. Kleuss, A. G. Gilman

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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
Issue number12
StatePublished - Jun 10 1997


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