Crowell Dring N, Huizinga David H
Department of Biological Sciences, Idaho State University, Pocatello, ID 83209, USA.
Trends Plant Sci. 2009 Mar;14(3):163-70. doi: 10.1016/j.tplants.2008.12.001. Epub 2009 Feb 7.
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.
蛋白质异戊烯化是指一个含15个碳原子的法尼基或含20个碳原子的香叶基香叶基部分与羧基末端或其附近的半胱氨酸残基共价连接。这种翻译后脂质修饰介导蛋白质-膜和蛋白质-蛋白质相互作用，对于脱落酸和生长素信号传导、分生组织发育及其他基本过程的正常调控是必需的。最近的研究还揭示了蛋白质异戊烯化在细胞分裂素生物合成和先天免疫中的作用。大多数异戊烯化蛋白会通过羧基末端蛋白水解和甲基化进一步修饰，总体而言，这些修饰对于异戊烯化蛋白的靶向定位和功能是必需的。
