Protein isoprenylation: the fat of the matter

• Published in: Trends in plant science Vol. 14; no. 3; pp. 163 - 170
• Main Authors: Crowell, Dring N., Huizinga, David H.
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier Ltd 01-03-2009; [Kidlington, Oxford, UK]: Elsevier Science Ltd; Elsevier
• Subjects: abscisic acid; Arabidopsis - enzymology; Arabidopsis - genetics; Arabidopsis - ultrastructure; auxins; Biological and medical sciences; cytokinins; Fundamental and applied biological sciences. Psychology; isoprenoids; isoprenylation; lipoproteins; literature reviews; methylation; plant proteins; Plant Proteins - metabolism; post-translational modification; Protein Prenylation; Protein Processing, Post-Translational; protein-protein interactions; proteolysis; signal transduction; Protein; Plant sciences
• ISSN: 1360-1385; 1878-4372
• DOI: 10.1016/j.tplants.2008.12.001

Protein isoprenylation refers to the covalent attachment of a 15-carbon farnesyl or 20-carbon geranylgeranyl moiety to a cysteine residue at or near the carboxyl terminus. This post-translational lipid modification, which mediates protein–membrane and protein–protein interactions, is necessary for normal control of abscisic acid and auxin signaling, meristem development, and other fundamental processes. Recent studies have also revealed roles for protein isoprenylation in cytokinin biosynthesis and innate immunity. Most isoprenylated proteins are further modified by carboxyl terminal proteolysis and methylation and, collectively, these modifications are necessary for the targeting and function of isoprenylated proteins.