The mechanism and functional roles of protein palmitoylation in the nervous system
The mechanism and functional roles of protein palmitoylation in the nervous system
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DOI：
10.1055/s-2007-973660
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发表时间：
1997-02-01
期刊：
影响因子：
1.4
通讯作者：
Bizzozero, OA
中科院分区：
文献类型：
--
作者：
Bizzozero, OA
棕榈酰化是指长链脂肪酸(主要是棕榈酸)共价连接到蛋白质半胱氨酸残基的侧链上。近年来，大量与神经系统功能相关的蛋白质，包括离子通道、神经递质受体、信号转导元件和细胞黏附分子等被发现是棕榈酰化的。然而，这些蛋白质中的脂肪酸缺乏普遍和明确的作用，这使得棕榈酰化在神经系统功能中的重要性受到了质疑。去年，人们发现棕榈酰蛋白硫酯酶(PPT)的缺乏是婴儿神经元蜡样脂褐素沉着症(INCL)的根本原因。这一发现不仅在阐明INCL的发病机制方面向前迈进了一步，而且也为寻找蛋白质棕榈酰化的功能(S)提供了新的动力。这项工作简明扼要地概述了动态酰化反应中涉及的分子机制和这种修饰的潜在生物学作用(S)，并对本问题中专门涉及INCL发病机制的那些介绍进行了介绍。
Palmitoylation refers to the covalent attachment of long-chain fatty acids, mostly palmitic acid, to the side chain of cysteine residues of proteins. In recent years, a considerable number of functionally relevant nervous system proteins including ion channels, neurotransmitter receptors, signal transduction components and cell-adhesion molecules have been found to be palmitoylated. However, the lack of a generalized and unambiguous role for the fatty acids in these proteins has questioned the importance of palmitoylation in the functioning of the nervous system. Last year, it was found that the deficiency of palmitoyl-protein thioesterase (PPT), one of the enzymes responsible for the removal of palmitate from proteins, is the underlying cause of infantile neuronal ceroid lipofuscinosis (INCL). This finding not only constitutes a step forward in elucidating the pathogenesis of INCL, but it also provides new impetus in the search for the function(s) of protein palmitoylation. This work succinctly outlines the molecular mechanisms involved in dynamic acylation and the potential biological role(s) of this modification, and it constitutes an introduction to those presentations in this issue which specifically deal with the pathogenic mechanisms of INCL.