Weak functional constraints on phosphoproteomes
Weak functional constraints on phosphoproteomes
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DOI：
10.1016/j.tig.2009.03.003
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发表时间：
2009-05-01
影响因子：
11.4
通讯作者：
Michnick, Stephen W.
中科院分区：
文献类型：
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作者：
Landry, Christian R.;Levy, Emmanuel D.;Michnick, Stephen W.
由于磷酸化位点在调节蛋白质功能中的重要作用，预期它们在进化上是保守的。然而，关于这一预测的结果喜忧参半。我们解决这些对比的结论表明，磷酸化，平均而言，更保守的非磷酸化的等效残基时，他们的富集在无序的蛋白质区域被考虑在内。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更加保守，这表明磷酸化蛋白质组的明显快速进化是由于大部分磷酸化位点没有功能。我们的研究结果强调了需要使用进化信息来识别功能调控特征，如真核蛋白质组的翻译后修饰。
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.