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PMID: 7708760 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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 ·Vol. 92 ·No. 7 ·1995-03-28 ·Pages 2984-8

Bhattacharya S, Chen L, Broach JR, Powers S

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.

MeSH Terms
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
Chemicals
Fungal Proteins Palmitic Acids Palmitic Acid Cyclic AMP GTP-Binding Proteins ras Proteins Glucose
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Bhattacharya S
Department of Molecular Biology, Princeton University, NJ 08544, USA.
Chen L
Broach J R
Powers S
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44 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.92.7.2984
Published
1995-03-28
Pages
2984-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC42343
Subset
IM
Grants
NCI NIH HHS · CA41086 · United States
External Links
PubMed source DOI: 10.1073/pnas.92.7.2984 PMC Full Text View journal details
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