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Science 13 July 1990:
Vol. 249. no. 4965, pp. 165 - 169
DOI: 10.1126/science.1695391

Articles

Science, Vol 249, Issue 4965, 165-169
Copyright © 1990 by American Association for the Advancement of Science


articles

Common modifications of trimeric G proteins and ras protein: involvement of polyisoprenylation

AA Finegold, WR Schafer, J Rine, M Whiteway, and F Tamanoi

Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637.

The heterotrimeric guanine nucleotide-binding regulatory proteins act at the inner surface of the plasma membrane to relay information from cell surface receptors to effectors inside the cell. These G proteins are not integral membrane proteins, yet are membrane associated. The processing and function of the gamma subunit of the yeast G protein involved in mating-pheromone signal transduction was found to be affected by the same mutations that block ras processing. The nature of these mutations implied that the gamma subunit was polyisoprenylated and that this modification was necessary for membrane association and biological activity. A microbial screen was developed for pharmacological agents that inhibit polyisoprenylation and that have potential application in cancer therapy.


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Comprehensive evaluation of isoprenoid biosynthesis regulation in Saccharomyces cerevisiae utilizing the Genome Reporter Matrix(TM).
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Molecular Characterization of Ste20p, a Potential Mitogen-activated Protein or Extracellular Signal-regulated Kinase Kinase (MEK) Kinase Kinase from Saccharomycescerevisiae.
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Enzymatic coupling of cholesterol intermediates to a mating pheromone precursor and to the ras protein.
W. Schafer, C. Trueblood, C. Yang, M. Mayer, S Rosenberg, C. Poulter, S. Kim, and J Rine (1990)
Science 249, 1133-1139
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Science. ISSN 0036-8075 (print), 1095-9203 (online)