Meinnel Thierry, Giglione Carmela
Protein Maturation, Cell Fate and Therapeutics, ISV, UPR2355, Centre National de la Recherche Scientifique, Batiment 23, 1 avenue de la Terrasse, F-91198 Gif-sur-Yvette cedex, France.
Front Biosci. 2008 May 1;13:6326-40. doi: 10.2741/3157.
Protein lipidation is a crucial protein modification involving the attachment of hydrophobic carbon skeletons (C:14-C:60) of various lipid classes--fatty acids, sterols, glycero-, phospho- and glycolipids. The lipid-protein bond frequently (i) involves the N- or C-terminal ends of the target, (ii) requires amide, ether or ester bonds to a small aminoacid, usually Gly or Cys and (iii) depends on proteolytic events. Lipidation results in protein targeting to the membrane, with the protein behaving as a peripheral component and being oriented toward the inside or outside of the cell. The addition of a single lipid is not sufficient for membrane targeting and another signal, often involving additional lipidation, is required. The methods available for predicting lipid modifications to proteins highlight the importance of identifying short protein motifs in a field in which few data are currently available, due to the complex nature of the modification. Full proteome annotation is already feasible with these predictive tools. We show that lipidation may affect 2-4 percent of all proteins in a given proteome and that double-lipidation is widespread.
蛋白质脂化是一种关键的蛋白质修饰，涉及多种脂质类别的疏水碳骨架（C:14 - C:60）——脂肪酸、固醇、甘油脂、磷脂和糖脂的附着。脂 - 蛋白键通常（i）涉及靶标的N端或C端，（ii）需要与一个小氨基酸（通常是甘氨酸或半胱氨酸）形成酰胺键、醚键或酯键，并且（iii）依赖于蛋白水解事件。脂化导致蛋白质靶向到膜上，蛋白质作为外周成分，其方向朝向细胞内部或外部。添加单个脂质不足以实现膜靶向，还需要另一个信号，通常涉及额外的脂化。由于修饰的复杂性，目前在该领域几乎没有可用数据，现有的预测蛋白质脂质修饰的方法突出了识别短蛋白质基序的重要性。使用这些预测工具进行全蛋白质组注释已经可行。我们表明，脂化可能影响给定蛋白质组中所有蛋白质的2% - 4%，并且双脂化很普遍。
