G蛋白偶联受体(G-protein-coupled receptors，GPCRs)作为跨膜蛋白，其结构和功能同时受相互作用的蛋白质和脂质分子调控. S-棕榈酰化（S-palmitoylation）能够影响GPCRs与信号蛋白及膜脂分子的相互作用，在GPCRs相关的多项生理进程中发挥重要调节作用. 棕榈酸与GPCRs的半胱氨酸间形成不稳定的硫酯键，其修饰动力学过程受棕榈酰转移酶（protein acly transferases，PATs）与硫酯酶（thioesterases）之间的可逆性双重调控，与受体活性及生理状态密切相关. 棕榈酰化修饰多发生在GPCRs的C末端，通过棕榈酸侧链插入到质膜内侧而形成第4和/或第5个胞内环，从而影响GPCRs的构象，促进其正确折叠与成熟，并对GPCRs胞内转运、分选、下游信号转导、失敏、内化、寡聚化等活动产生影响. 此外，棕榈酰化还与磷酸化、泛素化及亚硝基化等多种翻译后修饰机制相互作用，共同参与调节GPCRs的功能. GPCRs的棕榈酰化修饰酶学机制以及GPCRs蛋白复合体棕榈酰化修饰胞内动力学过程将是未来的研究热点.

G-protein-coupled receptors (GPCRs) are transmembrane proteins, hence a number of their structural and functional features are modulated by both proteins and lipids. S-palmitoylation, as a classical lipid modification, regulates diverse aspects of GPCRs by affecting the interaction between GPCRs and signal proteins or lipid molecules. It is defined as the addition of saturated 16-carbon palmitate acid to specific cysteine residues through the formation of a liable thioester bond. The palmitoylation/depalmitoylation dynamics is regulated reversibly by both the palmitoyl acyl transferases (PATs) and palmitoyl protein thioesterases under various physiological status. Many GPCRs are palmitoylated on cysteine residues present in their cytoplasmic termini. The insertion of palmitate into the cytoplasmic leaflet of the plasma membrane can create the fouth and/or the fifth intracellular loop, thus profoundly affecting GPCRs structure, trafficking, sorting, signaling, desensitisation, internalization and oligomerisation. Furthermore, the interplay between palmitoylation and other posttranslational modifications, such as phosphorylation, ubiquitination and nitrosylation, can regulate the function of GPCRs coordinatively. It is expected that the identification of enzymes involved in GPCRs palmitoylation dynamics will be a key to delineate the role of palmitoylation in regulating GPCRs functions.