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

Pedro Beltrao, Peer Bork, Nevan J. Krogan and 1 more

Molecular Systems Biology · 2013 · Review · CC BY-NC-SA

doi:10.1002/msb.201304521

Abstract

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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    Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C (2013 ) Acetyl‐phosphate is a critical determinant of lysine acetylation in E. coli. Mol Cell51: 265–272

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    Woodsmith J, Kamburov A, Stelzl U (2013 ) Dual coordination of post translational modifications in human protein networks. PLoS Comput Biol9: e1002933

    Not in our library10.1371/journal.pcbi.1002933

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    Wu R, Haas W, Dephoure N, Huttlin EL, Zhai B, Sowa ME, Gygi SP (2011 ) A large‐scale method to measure absolute protein phosphorylation stoichiometries. Nat Methods8: 677–683

    Not in our library10.1038/nmeth.1636

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    Wu X, Vellaichamy A, Wang D, Zamdborg L, Kelleher NL, Huber SC, Zhao Y (2013 ) Differential lysine acetylation profiles of Erwinia amylovora strains revealed by proteomics. J Proteomics79: 60–71

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    Xin X, Gfeller D, Cheng J, Tonikian R, Sun L, Guo A, Lopez L, Pavlenco A, Akintobi A, Zhang Y, Rual J‐F, Currell B, Seshagiri S, Hao T, Yang X, Shen YA, Salehi‐Ashtiani K, Li J, Cheng AT, Bouamalay D et al (2013 ) SH3 interactome conserves general function over specific form. Mol Syst Biol9: 1–17

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    Zanzoni A, Carbajo D, Diella F, Gherardini PF, Tramontano A, Helmer‐Citterich M, Via A (2011 ) Phospho3D 2.0: an enhanced database of three‐dimensional structures of phosphorylation sites. Nucleic Acids Res39: D268–D271

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    Not in our library10.1074/mcp.m800187-mcp200

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    Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z (2013 ) Comprehensive profiling of protein lysine acetylation in Escherichia coli. J Proteome Res12: 844–851

    Not in our library10.1021/pr300912q

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    Zielinska DF, Gnad F, Schropp K, Wiśniewski JR, Mann M (2012 ) Mapping N‐glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell46: 542–548

    Not in our library10.1016/j.molcel.2012.04.031

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    Zlocowski N, Sendra VG, Lorenz V, Villarreal MA, Jorge A, Núñez Y, Bennett EP, Clausen H, Nores GA, Irazoqui FJ (2011 ) Catalytic and glycan‐binding abilities of ppGalNAc‐T2 are regulated by acetylation. Biochem Biophys Res Commun410: 140–145

    Not in our library10.1016/j.bbrc.2011.05.125

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