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

Molecular Systems Biology

Pedro Beltrao³  Peer Bork²  Nevan J. Krogan¹ 

[1] Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California, USA;Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany;European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Cambridge, UK

关键词: acetylation;    evolution;    phosphorylation;    post‐translational modifications;    PTM cross‐talk;   

DOI  :  10.1002/msb.201304521

来源: Wiley

【 摘 要 】

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.

【 授权许可】

CC BY-NC-SA   
© 2013 The Authors

Creative Commons Attribution License, which permits distribution, and reproduction in any medium, provided the original author and source are credited. This license does not permit commercial exploitation without specific permission.