ArticleMolecular biology of the cell2000
Dual lipid modification motifs in G(alpha) and G(gamma) subunits are required for full activity of the pheromone response pathway in Saccharomyces cerevisiae.
Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 61 citations in OpenAlex.
- A molecular dynamics study of membrane positioning for 7-transmembrane RGS proteins to modulate G-protein-mediated signaling in plants.Computational and structural biotechnology journal · 2025Article
- Article
- Aggregation and Prion-Inducing Properties of the G-Protein Gamma Subunit Ste18 are Regulated by Membrane Association.International journal of molecular sciences · 2020Article
- Regulation of large and small G proteins by ubiquitination.The Journal of biological chemistry · 2019Review
- Expression of varied GFPs in Saccharomyces cerevisiae: codon optimization yields stronger than expected expression and fluorescence intensity.Scientific reports · 2016Article
- Heterotrimeric G Protein-coupled Receptor Signaling in Yeast Mating Pheromone Response.The Journal of biological chemistry · 2016Review
- Gγ recruitment systems specifically select PPI and affinity-enhanced candidate proteins that interact with membrane protein targets.Scientific reports · 2015Article
- Specific α-arrestins negatively regulate Saccharomyces cerevisiae pheromone response by down-modulating the G-protein-coupled receptor Ste2.Molecular and cellular biology · 2014Article
- Desired alteration of protein affinities: competitive selection of protein variants using yeast signal transduction machinery.PloS one · 2014Article
- Yeast one-hybrid gγ recruitment system for identification of protein lipidation motifs.PloS one · 2013Article
- Article
- Dynamic localization of Fus3 mitogen-activated protein kinase is necessary to evoke appropriate responses and avoid cytotoxic effects.Molecular and cellular biology · 2010Article
- The beta subunit of the heterotrimeric G protein triggers the Kluyveromyces lactis pheromone response pathway in the absence of the gamma subunit.Molecular biology of the cell · 2010Article
- Chemical gradients and chemotropism in yeast.Cold Spring Harbor perspectives in biology · 2009Review
- G Protein Mono-ubiquitination by the Rsp5 Ubiquitin Ligase.The Journal of biological chemistry · 2009Article
- Ggamma1 + Ggamma2 not equal to Gbeta: heterotrimeric G protein Ggamma-deficient mutants do not recapitulate all phenotypes of Gbeta-deficient mutants.Plant physiology · 2008Article
- Article
- Mapping dynamic protein interactions in MAP kinase signaling using live-cell fluorescence fluctuation spectroscopy and imaging.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- The cAMP pathway is important for controlling the morphological switch to the pathogenic yeast form of Paracoccidioides brasiliensis.Molecular microbiology · 2007Article
- Function and regulation in MAPK signaling pathways: lessons learned from the yeast Saccharomyces cerevisiae.Biochimica et biophysica acta · 2007Review
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4 authors at 1 institution in 1 country.
Funding
Abstract
To establish the biological function of thioacylation (palmitoylation), we have studied the heterotrimeric guanine nucleotide-binding protein (G protein) subunits of the pheromone response pathway of Saccharomyces cerevisiae. The yeast G protein gamma subunit (Ste18p) is unusual among G(gamma) subunits because it is farnesylated at cysteine 107 and has the potential to be thioacylated at cysteine 106. Substitution of either cysteine results in a strong signaling defect. In this study, we found that Ste18p is thioacylated at cysteine 106, which depended on prenylation of cysteine 107. Ste18p was targeted to the plasma membrane even in the absence of prenylation or thioacylation. However, G protein activation released prenylation- or thioacylation-defective Ste18p into the cytoplasm. Hence, lipid modifications of the G(gamma) subunit are dispensable for G protein activation by receptor, but they are required to maintain the plasma membrane association of G(betagamma) after receptor-stimulated release from G(alpha). The G protein alpha subunit (Gpa1p) is tandemly modified at its N terminus with amide- and thioester-linked fatty acids. Here we show that Gpa1p was thioacylated in vivo with a mixture of radioactive myristate and palmitate. Mutation of the thioacylation site in Gpa1p resulted in yeast cells that displayed partial activation of the pathway in the absence of pheromone. Thus, dual lipidation motifs on Gpa1p and Ste18p are required for a fully functional pheromone response pathway.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.