| Title: | Pheromone action regulates G-protein alpha-subunit myristoylation in the yeast Saccharomyces cerevisiae |
| Author(s): | Dohlman HG; Goldsmith P; Spiegel AM; Thorner J; |
| Address: | "Department of Molecular and Cell Biology, University of California, Berkeley 94720" |
| ISSN/ISBN: | 0027-8424 (Print) 1091-6490 (Electronic) 0027-8424 (Linking) |
| Abstract: | "Myristic acid (C14:0) is added to the N-terminal glycine residue of the alpha subunits of certain receptor-coupled guanine nucleotide-binding regulatory proteins (G proteins). The G alpha subunit (GPA1 gene product) coupled to yeast pheromone receptors exists as a pool of both myristoylated and unmyristolyated species. After treatment of MATa cells with alpha factor, the myristoylated form of Gpa1p increases dramatically, and the unmyristoylated form decreases concomitantly. This pheromone-stimulated shift depends on the function of STE2 (alpha-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 G alpha-G beta gamma association and receptor coupling, pheromone-dependent stimulation of Gpa1p myristoylation may be an important contributing factor in adaptation after signal transmission" |
| Keywords: | "Amino Acid Sequence GTP-Binding Proteins/chemistry/immunology/*metabolism Genes, Fungal Mating Factor Molecular Sequence Data Myristates/*metabolism Peptides/chemistry/immunology/physiology Pheromones/*physiology Protein Processing, Post-Translational Sac;" |
| Notes: | "MedlineDohlman, H G Goldsmith, P Spiegel, A M Thorner, J eng GM21841/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1993/10/15 Proc Natl Acad Sci U S A. 1993 Oct 15; 90(20):9688-92. doi: 10.1073/pnas.90.20.9688" |
