Biochemistry of protein prenylation.
Biochemistry of protein prenylation.
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发表时间：
1992-12
影响因子：
6.5
通讯作者：
Patrick J. Casey
中科院分区：
文献类型：
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作者：
Patrick J. Casey
类异戊二烯脂质的共价修饰（异戊二烯化）现在被认为是促进膜相互作用和各种细胞蛋白质生物活性的机制。15-碳法呢基和20-碳香叶基香叶基类异戊二烯都参与了这些修饰，这些修饰发生在蛋白质的羧基末端半胱氨酸残基上（图1）。已知的异戊二烯化蛋白包括核蛋白核纤层蛋白B和许多负责控制广谱信号转导途径的GTP结合调节蛋白（G蛋白）。本文综述了蛋白质异戊烯化的发展和最新研究，特别强调了所涉及过程的生物化学。其他几个最近的评论可用于更详细的覆盖面的方面，在这里得到有限的关注（1-3）。
Covalent modification by isoprenoid lipids (prenylation) is now recognized as a mechanism to promote membrane interactions and biological activities of a variety of cellular proteins. Both the 15-carbon farnesyl and 20-carbon geranylgeranyl isoprenoids are involved in these modifications, which occur on carboxyl-terminal cysteine residues of proteins (Fig. 1). Known prenylated proteins include the nuclear protein lamin B and a number of GTP-binding regulatory proteins (G proteins) responsible for controlling a wide spectrum of signal transduction pathways. This review summarizes the development of, and recent studies in, the field of protein prenylation, with particular emphasis on the biochemistry of the processes involved. Several other recent reviews are available for more detailed coverage of aspects which receive limited attention here (1-3).