蛋白磷酸化在控制細(xì)胞信號傳導(dǎo)中無處不在,。純化和特征化磷酸的改良方法使磷酸化位點數(shù)據(jù)爆炸性增長,，我們現(xiàn)在可以探討蛋白磷酸化如何發(fā)展的。這個問題在本文中已得到解決,。（1）酪氨酸殘基（可磷酸化）在后生動物的進(jìn)化中已選擇性丟失,。（2）快速進(jìn)化、無序的蛋白質(zhì)區(qū)域中大多數(shù)磷酸化位點改變了位置,。（生物谷Bioon.com）
生物谷推薦原始出處：
Science 25 September 2009:DOI: 10.1126/science.1180331
Evolving Cell Signals
Mark O. Collins
Protein phosphorylation has emerged as a ubiquitous regulatory switch in cell signaling networks. Improved methods to purify and characterize phosphopeptides have led to an explosion of phosphorylation site data, and we can now explore how protein phosphorylation evolved. This question has been tackled by two studies in this issue. On page 1686, Tan et al. (1) report that tyrosine residues (which can be phosphorylated) have been selectively lost through metazoan evolution. On page 1682, Holt et al. (2) show that most phosphorylation sites shift position in rapidly evolving, disordered regions of proteins.
Proteomic Mass Spectrometry Group, The Wellcome Trust Sanger Institute, Hinxton, Cambridge CB10 1SA, UK.
