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

C. Kleuss, A. G. Gilman

Research output: Contribution to journalArticle

41 Citations (Scopus)

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 G(α) protein that activates adenylyl cyclase, α(s), is not myristoylated but can be reversibly palmitoylated. It appears that α(s) 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. Palmiloylation of native α(s), 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 - 1997

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Adenylyl Cyclases
GTP-Binding Proteins
Palmitates
Protein Subunits
Myristic Acid
Cysteine
Proteins

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

G(sα) contains an unidentified covalent modification that increases its affinity for adenylyl cyclase. / Kleuss, C.; Gilman, A. G.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 94, No. 12, 1997, p. 6116-6120.

Research output: Contribution to journalArticle

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