Meinnel Thierry, Dian Cyril, Giglione Carmela
Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198, Gif-sur-Yvette, France.
Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198, Gif-sur-Yvette, France.
Trends Biochem Sci. 2020 Jul;45(7):619-632. doi: 10.1016/j.tibs.2020.03.007. Epub 2020 Apr 15.
N-myristoylation (MYR) is a crucial fatty acylation catalyzed by N-myristoyltransferases (NMTs) that is likely to have appeared over 2 billion years ago. Proteome-wide approaches have now delivered an exhaustive list of substrates undergoing MYR across approximately 2% of any proteome, with constituents, several unexpected, associated with different membrane compartments. A set of <10 proteins conserved in eukaryotes probably represents the original set of N-myristoylated targets, marking major changes occurring throughout eukaryogenesis. Recent findings have revealed unexpected mechanisms and reactivity, suggesting competition with other acylations that are likely to influence cellular homeostasis and the steady state of the modification landscape. Here, we review recent advances in NMT catalysis, substrate specificity, and MYR proteomics, and discuss concepts regarding MYR during evolution.
N-肉豆蔻酰化（MYR）是由N-肉豆蔻酰转移酶（NMT）催化的一种关键的脂肪酰化作用，这种作用可能在20多亿年前就已出现。全蛋白质组学方法现已给出了一份详尽的经历MYR修饰的底物清单，这些底物约占任何蛋白质组的2%，其成分与不同的膜区室相关，其中有几种是意想不到的。一组在真核生物中保守的少于10种的蛋白质可能代表了最初的N-肉豆蔻酰化靶标集，标志着整个真核生物起源过程中发生的重大变化。最近的研究结果揭示了意想不到的机制和反应活性，表明与其他可能影响细胞内稳态和修饰格局稳态的酰化作用存在竞争。在此，我们综述了NMT催化、底物特异性和MYR蛋白质组学方面的最新进展，并讨论了进化过程中有关MYR的概念。
