Evolution and functional cross-talk of protein post-translational modifications

被引：277
作者：
Beltrao, Pedro [1 ]
Bork, Peer [2 ,3 ]
Krogan, Nevan J. [4 ,5 ,6 ]
van Noort, Vera [2 ]
机构：
[1] European Bioinformat Inst EMBL EBI, European Mol Biol Lab, Cambridge, England
[2] European Mol Biol Lab, Struct & Computat Biol Unit, D-69012 Heidelberg, Germany
[3] Max Delbruck Ctr Mol Med, Berlin, Germany
[4] Univ Calif San Francisco, Dept Cellular & Mol Pharmacol, San Francisco, CA 94143 USA
[5] Calif Inst Quantitat Biosci, San Francisco, CA USA
[6] J David Gladstone Inst, San Francisco, CA USA
来源：
MOLECULAR SYSTEMS BIOLOGY | 2013年 / 9卷
基金：
美国国家卫生研究院;
关键词：
acetylation; evolution; phosphorylation; post-translational modifications; PTM cross-talk; LYSINE ACETYLATION; PHOSPHORYLATION SITES; COMPARATIVE GENOMICS; NATURAL-HISTORY; GLOBAL ANALYSIS; UBIQUITIN; REVEALS; KINASE; NETWORKS; TARGETS;
D O I：
10.1002/msb.201304521
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Protein post-translational modifications (PTMs) allow the cell to regulate protein activity and play a crucial role in the response to changes in external conditions or internal states. Advances in mass spectrometry now enable proteome wide characterization of PTMs and have revealed a broad functional role for a range of different types of modifications. Here we review advances in the study of the evolution and function of PTMs that were spurred by these technological improvements. We provide an overview of studies focusing on the origin and evolution of regulatory enzymes as well as the evolutionary dynamics of modification sites. Finally, we discuss different mechanisms of altering protein activity via post-translational regulation and progress made in the large-scale functional characterization of PTM function.
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页数：13
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