| Title: | A role for isoprenoid lipids in the localization and function of an oncoprotein |
| Address: | "Department of Molecular and Cellular Biology, University of California, Berkeley 94720" |
| ISSN/ISBN: | 1043-4674 (Print) 1043-4674 (Linking) |
| Abstract: | "Intermediates of the cholesterol biosynthetic pathway are covalently attached to a number of eukaryotic proteins, including the Ras oncoprotein. Ras protein is post-translationally processed at its carboxyl terminus in three steps, resulting in a COOH-terminal cysteine residue to which a polyisoprenoid moiety, probably farnesyl, is attached in a thioether linkage. Polyisoprenylation of Ras protein is required for its membrane association and for the oncogenicity of mutant forms of the protein. Inhibition of polyisoprenylation may offer a route by which Ras-mediated tumors can be pharmacologically suppressed. Other proteins that are polyisoprenylated include nuclear lamin B, fungal mating factors, and subunits of trimeric guanine nucleotide-binding proteins. A consensus sequence for polyisoprenylation (Cys-aliphatic-aliphatic-X) has been identified at the COOH-terminus of modified proteins. Recent evidence indicates that proteins can be modified by several different polyisoprenoids" |
| Keywords: | Amino Acid Sequence Binding Sites Cell Division/physiology Cell Membrane/metabolism Fungal Proteins/genetics/metabolism *Lipid Metabolism Molecular Sequence Data Oncogene Proteins/genetics/*metabolism Pheromones/metabolism *ras Proteins; |
| Notes: | "MedlineRine, J Kim, S H eng CA-45593/CA/NCI NIH HHS/ GM31105/GM/NIGMS NIH HHS/ GM35827/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review 1990/03/01 New Biol. 1990 Mar; 2(3):219-26" |
