Ubiquitination of substrates by esterification.
Ubiquitination of substrates by esterification.
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DOI：
10.1111/j.1600-0854.2011.01269.x
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发表时间：
2012-01
期刊：
影响因子：
--
通讯作者：
Hansen TH
中科院分区：
文献类型：
--
作者：
Wang X;Herr RA;Hansen TH
翻译后泛素化修饰决定了许多蛋白质的细胞内定位和命运，从而影响了多种生理功能。过去的教条是，泛素仅通过与内部赖氨酸残基的异肽键或较不常见的与N-末端的肽键与底物偶联。然而，令人费解的是，据报道，几种缺乏赖氨酸的蛋白质保留了泛素依赖的命运。最近的观察结果表明，底物的泛素化也可以通过硫代或氧代酯键的形成分别发生在半胱氨酸或丝氨酸和苏氨酸残基上（统称为酯化），从而解决了这一矛盾。虽然化学上是可能的，但这些键被认为太不稳定而不具有生理相关性。在这篇综述中，我们讨论了蛋白质底物通过酯化作用遍在化的最新证据，并推测其机制及其生理重要性。
Posttranslational modification by ubiquitination determines intracellular location and fate of numerous proteins thus impacting a diverse array of physiologic functions. Past dogma has been that ubiquitin was only coupled to substrates by isopeptide bonds to internal lysine residues or less frequently peptide bonds to the N-terminus. Enigmatically, however, several proteins lacking lysines had been reported to retain ubiquitin dependent fates. Resolution of this paradox was afforded by recent observations that ubiquitination of substrates can also occur on cysteine or serine and threonine residues by thio- or oxy-ester bond formation, respectively (collectively called esterification). Although chemically possible, these bonds were considered too labile to be of physiological relevance. In this review we discuss recent evidence for the ubiquitination of protein substrates by esterification and speculate on its mechanism and its physiological importance.
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