Progress toward Understanding Protein S-acylation: Prospective in Plants.
Progress toward Understanding Protein S-acylation: Prospective in Plants.
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DOI：
10.3389/fpls.2017.00346
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发表时间：
2017
影响因子：
5.6
通讯作者：
Qi B
中科院分区：
文献类型：
--
作者：
Li Y;Qi B
S-酰化，也称为S-棕榈酰化或棕榈酰化，是一种可逆的翻译后脂质修饰，其中长链脂肪酸，通常是16碳棕榈酸酯，通过硫酯键共价连接到整个蛋白质的半胱氨酸残基上。它参与了植物生长发育、繁殖和逆境反应等一系列重要的生物学过程。S-酰化是真核生物中普遍存在的机制，由称为蛋白质S-酰基转移酶（PATs）的酶家族催化。自2002年在酵母中发现第一个PAT以来，S-酰化的研究在哺乳动物系统中加速，随后在植物中也是如此。然而，这仍然是一个困难的领域，研究由于大量的PAT，甚至更大数量的假定S-酰化底物蛋白，他们修改在每个基因组。这与用于研究S-酰化的技术中的缺点相结合，例如，与蛋白质磷酸化相比，导致该领域的进展较慢。本文综述了近年来在蛋白质S-酰基转移酶和S-酰化蛋白的研究进展，以及PAT与酵母和哺乳动物特异性底物蛋白的相互作用机制。蛋白质S-酰化和PAT在植物中的研究也将包括在内，尽管这一领域目前在酵母和哺乳动物系统中的研究较少。
S-acylation, also known as S-palmitoylation or palmitoylation, is a reversible post-translational lipid modification in which long chain fatty acid, usually the 16-carbon palmitate, covalently attaches to a cysteine residue(s) throughout the protein via a thioester bond. It is involved in an array of important biological processes during growth and development, reproduction and stress responses in plant. S-acylation is a ubiquitous mechanism in eukaryotes catalyzed by a family of enzymes called Protein S-Acyl Transferases (PATs). Since the discovery of the first PAT in yeast in 2002 research in S-acylation has accelerated in the mammalian system and followed by in plant. However, it is still a difficult field to study due to the large number of PATs and even larger number of putative S-acylated substrate proteins they modify in each genome. This is coupled with drawbacks in the techniques used to study S-acylation, leading to the slower progress in this field compared to protein phosphorylation, for example. In this review we will summarize the discoveries made so far based on knowledge learnt from the characterization of protein S-acyltransferases and the S-acylated proteins, the interaction mechanisms between PAT and its specific substrate protein(s) in yeast and mammals. Research in protein S-acylation and PATs in plants will also be covered although this area is currently less well studied in yeast and mammalian systems.