Morello J P, Bouvier M
Département de biochimie, Faculté de Médecine, Université de Montréal, QC, Canada.
Biochem Cell Biol. 1996;74(4):449-57. doi: 10.1139/o96-049.
Protein acylation is a post-translational modification that has seized much attention in the last few years. Depending on the nature of the fatty acid added, protein acylation can take the form of palmitoylation, myristoylation, or prenylation. Palmitoylation has been implicated in the modification of several different proteins and is particularly prevalent in G-protein coupled receptors and their cognate G-proteins, where it is thought to have an important regulatory function. Given that palmitoylation of these proteins is a dynamic phenomenon in which turnover rate is modulated by agonist activation, it is thought to be implicated in processes such as receptor phosphorylation and desensitization as well as in G-protein membrane translocation. A better understanding of the regulation of signal transduction mediated by G-protein coupled receptors will require the identification and characterization of those enzymes implicated in the palmitoylation and depalmitoylation process of this large class of receptors and their signalling allies.
蛋白质酰化是一种翻译后修饰,在过去几年中备受关注。根据所添加脂肪酸的性质,蛋白质酰化可以采取棕榈酰化、肉豆蔻酰化或异戊二烯化的形式。棕榈酰化与几种不同蛋白质的修饰有关,在G蛋白偶联受体及其同源G蛋白中尤为普遍,人们认为它在其中具有重要的调节功能。鉴于这些蛋白质的棕榈酰化是一种动态现象,其周转速率受激动剂激活调节,因此人们认为它与受体磷酸化和脱敏以及G蛋白膜易位等过程有关。要更好地理解由G蛋白偶联受体介导的信号转导调控,就需要鉴定和表征那些参与这类大量受体及其信号转导伙伴的棕榈酰化和去棕榈酰化过程的酶。