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

期刊

MOLECULAR SYSTEMS BIOLOGY
卷 9, 期 -, 页码 -

出版社

WILEY
DOI: 10.1002/msb.201304521

关键词

acetylation; evolution; phosphorylation; post-translational modifications; PTM cross-talk

资金

  1. US National Institutes of Health [P50GM082250, R01GM084448, P01AI090935, P50GM081879, R01GM098101, R01GM084279, P01AI091575]
  2. Defense Advanced Research Projects Agency [DAR-PA-10-93-Prophecy-PA-008]
  3. Human Frontier Science Program [CDA00069/2013-C]

向作者/读者索取更多资源

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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