Pheromone action regulates G-protein α-subunit myristoylation in the yeast Saccharomyces cerevisiae

Henrik G. Dohlman, Paul Goldsmith, Allen M. Spiegel, Jeremy Thorner

Research output: Contribution to journalArticlepeer-review

54 Scopus citations


Myristic acid (C14:0) is added to the N-terminal glycine residue of the α subunits of certain receptor-coupled guanine nucleotide-binding regulatory proteins (G proteins). The Ga subunit (GPA1 gene product) coupled to yeast pheromone receptors exists as a pool of both myristoylated and unmyristoylated species. After treatment of MATa cells with α factor, the myristoylated form of Gpa1p increases dramatically, and the unmyristoylated form decreases concomitantly. This pheromone-stimulated shift depends on the function of STE2 (α-factor receptor), STE11 (a protein kinase in the response pathway), and NMT1 (myristoyl-CoA:protein N-myristoyltransferase) genes and uses the existing pool of fatty acids (is not blocked by cerulenin). Myristoylated Gpa1p persists long after pheromone is removed. Because myristoylation is essential for proper Gα-Gβγ association and receptor coupling, pheromone-dependent stimulation of Gpa1p myristoylation may be an important contributing factor in adaptation after signal transmission.

Original languageEnglish (US)
Pages (from-to)9688-9692
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number20
StatePublished - Oct 15 1993
Externally publishedYes


  • Adaptation
  • Mutants
  • Posttranslational modification

ASJC Scopus subject areas

  • General


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