Cellular Neurophysiology, Hannover Medical School, Carl-Neuberg-Strasse 1, Hannover 30625, Germany.
Biochem Soc Trans. 2013 Feb 1;41(1):89-94. doi: 10.1042/BST20120235.
The covalent attachment of palmitic acid to one or more cysteine residues (S-palmitoylation) is a widespread modification of signalling proteins. With the finding that palmitoylation is a dynamic process, it is now widely accepted that repeated cycles of palmitoylation/depalmitoylation could be involved in the regulation of multiple signalling processes. Palmitoylation also represents a common post-translational modification of the GPCRs (G-protein-coupled receptors). Functionally, palmitoylation of GPCRs has been shown to play a central role in the regulation of multiple receptor functions, including determining the efficiency and selectivity of G-protein coupling, receptor phosphorylation and desensitization, endocytosis and transport to the plasma membrane. The present review summarizes our current knowledge of the palmitoylation of serotonin (5-hydroxytryptamine) receptors and its role in the regulation of receptor functions.
棕榈酸与一个或多个半胱氨酸残基的共价连接（S-棕榈酰化）是信号蛋白的一种广泛修饰。随着棕榈酰化是一个动态过程的发现，现在人们普遍认为，棕榈酰化/去棕榈酰化的反复循环可能参与了多种信号过程的调节。棕榈酰化也是 G 蛋白偶联受体（GPCRs）的常见翻译后修饰。从功能上讲，GPCR 的棕榈酰化已被证明在调节多种受体功能方面起着核心作用，包括确定 G 蛋白偶联的效率和选择性、受体磷酸化和脱敏、内吞作用以及向质膜的运输。本综述总结了我们目前对 5-羟色胺（5-羟色胺）受体棕榈酰化及其在调节受体功能中的作用的认识。
