title: Evolution and functional cross-talk of protein post-translational modifications.
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.
authors.affiliation: European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Cambridge, UK.
authors.forename: Pedro
authors.initials: P
authors.lastname: Beltrao
authors.forename: Peer
authors.initials: P
authors.lastname: Bork
authors.forename: Nevan J
authors.initials: NJ
authors.lastname: Krogan
authors.forename: Vera
authors.initials: V
authors.lastname: van Noort
mesh_terms: D000107:Acetylation; D030562:Databases, Protein; D019143:Evolution, Molecular; D013058:Mass Spectrometry; D010766:Phosphorylation; D010802:Phylogeny; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D040901:Proteomics
chemical_list: D011506:Proteins