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

Sharmila Bhattacharya, Li Chen, James R. Broach, Scott Powers

Research output: Contribution to journalArticle

67 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)2984-2988
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume92
Issue number7
DOIs
StatePublished - Mar 28 1995

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ras Proteins
Yeasts
Cell Membrane
Glucose
Membranes
Eukaryotic Cells
Protein Transport
Mutant Proteins
GTP-Binding Proteins
Adenylyl Cyclases
Saccharomyces cerevisiae
Signal Transduction
Proteins
Phenotype
Growth

All Science Journal Classification (ASJC) codes

  • General

Cite this

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Ras membrane targeting is essential for glucose signaling but not for viability in yeast. / Bhattacharya, Sharmila; Chen, Li; Broach, James R.; Powers, Scott.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 92, No. 7, 28.03.1995, p. 2984-2988.

Research output: Contribution to journalArticle

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