| Title: | Common modifications of trimeric G proteins and ras protein: involvement of polyisoprenylation |
| Author(s): | Finegold AA; Schafer WR; Rine J; Whiteway M; Tamanoi F; |
| Address: | "Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637" |
| ISSN/ISBN: | 0036-8075 (Print) 0036-8075 (Linking) |
| Abstract: | "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" |
| Keywords: | "Amino Acid Sequence Cell Membrane/metabolism Cloning, Molecular Epitopes/genetics GTP-Binding Proteins/genetics/*metabolism Hemagglutinins, Viral/immunology Lovastatin/pharmacology Mevalonic Acid/pharmacology Molecular Sequence Data Mutation Oncogene Prot;" |
| Notes: | "MedlineFinegold, A A Schafer, W R Rine, J Whiteway, M Tamanoi, F eng CA 41996/CA/NCI NIH HHS/ GM 07183/GM/NIGMS NIH HHS/ GM 35827/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. 1990/07/13 Science. 1990 Jul 13; 249(4965):165-9. doi: 10.1126/science.1695391" |
