Centro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC), CONICET, Universidad Nacional de Córdoba, Córdoba, Argentina.
Departamento de Química Biológica Ranwel Caputto, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Córdoba, Argentina.
Traffic. 2017 Nov;18(11):699-710. doi: 10.1111/tra.12510. Epub 2017 Sep 24.
Protein S-acylation, also known as palmitoylation, consists of the addition of a lipid molecule to one or more cysteine residues through a thioester bond. This modification, which is widespread in eukaryotes, is thought to affect over 12% of the human proteome. S-acylation allows the reversible association of peripheral proteins with membranes or, in the case of integral membrane proteins, modulates their behavior within the plane of the membrane. This review focuses on the consequences of protein S-acylation on intracellular trafficking and membrane association. We summarize relevant information that illustrates how lipid modification of proteins plays an important role in dictating precise intracellular movements within cells by regulating membrane-cytosol exchange, through membrane microdomain segregation, or by modifying the flux of the proteins by means of vesicular or diffusional transport systems. Finally, we highlight some of the key open questions and major challenges in the field.
蛋白质 S-酰化，也称为棕榈酰化，是指通过硫酯键将脂质分子添加到一个或多个半胱氨酸残基上。这种在真核生物中广泛存在的修饰被认为影响了超过 12%的人类蛋白质组。S-酰化允许外周蛋白与膜可逆地结合，或者在整合膜蛋白的情况下，调节它们在膜平面内的行为。这篇综述主要关注蛋白质 S-酰化对细胞内运输和膜结合的影响。我们总结了相关信息，说明了通过调节膜-细胞质交换、通过膜微区隔分离、或通过囊泡或扩散运输系统改变蛋白质的通量，蛋白质的脂质修饰如何在通过调节膜-细胞质交换、通过膜微区隔分离、或通过改变蛋白质的通量来精确控制细胞内运动方面发挥重要作用。最后，我们强调了该领域的一些关键问题和主要挑战。
