Ras membrane targeting is essential for glucose signaling but not for viability in yeast

Bhattacharya, S., Chen, L., Broach, J. R., Powers, S. (March 1995) Ras membrane targeting is essential for glucose signaling but not for viability in yeast. Proceedings of the National Academy of Sciences of the United States of America, 92 (7). pp. 2984-8. ISSN 0027-8424

URL: http://www.ncbi.nlm.nih.gov/pubmed/7708760

Abstract

Ras proteins are small GTP binding proteins that serve as critical relays in a variety of signal transduction pathways in eukaryotic cells. Like most metazoan Ras proteins, yeast Ras is post-translationally modified by addition of a farnesyl and a palmitoyl moiety, and these modifications are required for targeting the protein to the cytoplasmic face of the plasma membrane and for biological activity of the protein. We have constructed mutants of the yeast (Saccharomyces cerevisiae) Ras that are farnesylated in vivo but are not palmitoylated. These mutant proteins are not localized to the plasma membrane but function in the cell as well as the wild-type protein. Such mutants are viable but fail to induce a transient increase in intracellular cAMP concentration in response to glucose addition, although this deficiency does not yield a marked growth phenotype. These results are consistent with the hypothesis that the essential role of the farnesyl moiety on yeast Ras is to enhance productive interaction between Ras and its essential downstream target, adenylyl cyclase, rather than to localize Ras to the plasma membrane.

Item Type: Paper
Uncontrolled Keywords: Alleles Amino Acid Sequence Cyclic AMP/metabolism Fungal Proteins/biosynthesis/genetics/*metabolism GTP-Binding Proteins/metabolism Glucose/*metabolism Hot Temperature Introns Kinetics Molecular Sequence Data Mutagenesis Palmitic Acid Palmitic Acids/metabolism Plasmids Point Mutation Protein Prenylation Protein Processing, Post-Translational Saccharomyces cerevisiae/genetics/growth & development/*physiology *Signal Transduction Suppression, Genetic *ras Proteins
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > G protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > G protein > Ras
organism description > yeast
CSHL Authors:
Communities: CSHL labs > Powers lab
Depositing User: Matt Covey
Date: 28 March 1995
Date Deposited: 26 Feb 2014 16:35
Last Modified: 26 Feb 2014 16:35
PMCID: PMC42343
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29520

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