Manning Gerard, Plowman Gregory D, Hunter Tony, Sudarsanam Sucha
Sugen Inc. 230 East Grand Ave, South San Francisco, CA 94080, USA.
Trends Biochem Sci. 2002 Oct;27(10):514-20. doi: 10.1016/s0968-0004(02)02179-5.
Protein phosphorylation controls many cellular processes, especially those involved in intercellular communication and coordination of complex functions. To explore the evolution of protein phosphorylation, we compared the protein kinase complements ('kinomes') of budding yeast, worm and fly, with known human kinases. We classify kinases into putative orthologous groups with conserved functions and discuss kinase families and pathways that are unique, expanded or lost in each lineage. Fly and human share several kinase families involved in immunity, neurobiology, cell cycle and morphogenesis that are absent from worm, suggesting that these functions might have evolved after the divergence of nematodes from the main metazoan lineage.
蛋白质磷酸化控制着许多细胞过程，尤其是那些涉及细胞间通讯和复杂功能协调的过程。为了探究蛋白质磷酸化的进化，我们将出芽酵母、线虫和果蝇的蛋白激酶互补物（“激酶组”）与已知的人类激酶进行了比较。我们将激酶分类为具有保守功能的假定直系同源组，并讨论了在每个谱系中独特、扩展或缺失的激酶家族和信号通路。果蝇和人类共享几个参与免疫、神经生物学、细胞周期和形态发生的激酶家族，而线虫中则没有这些家族，这表明这些功能可能是在 nematodes 从主要后生动物谱系分化之后进化而来的。
