PMID: 9177179Jun 10, 1997Paper

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

Proceedings of the National Academy of Sciences of the United States of America
C Kleuss, A G Gilman

Abstract

Many G protein alpha subunits are dually acylated with myristate and palmitate or are palmitoylated on more than one cysteine residue near their N termini. The Galpha protein that activates adenylyl cyclase, alphas, is not myristoylated but can be reversibly palmitoylated. It appears that alphas 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 alphas does not account for its high affinity for adenylyl cyclase.

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Citations

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