Landry Christian R, Levy Emmanuel D, Michnick Stephen W
Centre Robert-Cedergren, Bio-Informatique et Génomique, Département de Biochimie, C.P. 6128, Succ. Centre-Ville, Montreal, Quebec H3C 3J7, Canada.
Trends Genet. 2009 May;25(5):193-7. doi: 10.1016/j.tig.2009.03.003. Epub 2009 Apr 6.
Owing to their crucial roles in regulating protein function, phosphorylation sites (phosphosites) are expected to be evolutionarily conserved. However, mixed results regarding this prediction have been reported. We resolve these contrasting conclusions to show that phosphosites are, on average, more conserved than non-phosphorylated equivalent residues when their enrichment in disordered regions of proteins is taken into account. Phosphosites of known function are dramatically more conserved than those with no characterized function, indicating that the apparent rapid evolution of phosphoproteomes results from a large fraction of phosphosites being non-functional. Our findings highlight the need to use evolutionary information to identify functional regulatory features such as post-translational modifications of eukaryotic proteomes.
由于磷酸化位点（磷酸化修饰位点）在调节蛋白质功能中发挥着关键作用，因此预计它们在进化过程中是保守的。然而，关于这一预测的结果却参差不齐。我们解决了这些相互矛盾的结论，结果表明，当考虑到磷酸化位点在蛋白质无序区域中的富集情况时，平均而言，磷酸化位点比未磷酸化的等效残基更保守。已知功能的磷酸化位点比那些没有特征功能的磷酸化位点保守得多，这表明磷酸化蛋白质组明显的快速进化是由于很大一部分磷酸化位点没有功能。我们的研究结果强调了利用进化信息来识别真核生物蛋白质组的功能调节特征（如翻译后修饰）的必要性。
