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Deciphering a global network of functionally associated post‐translational modifications
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Deciphering a global network of functionally associated post‐translational modifications
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Journal Article
Deciphering a global network of functionally associated post‐translational modifications
2012
Overview
Various post‐translational modifications (PTMs) fine‐tune the functions of almost all eukaryotic proteins, and co‐regulation of different types of PTMs has been shown within and between a number of proteins. Aiming at a more global view of the interplay between PTM types, we collected modifications for 13 frequent PTM types in 8 eukaryotes, compared their speed of evolution and developed a method for measuring PTM co‐evolution within proteins based on the co‐occurrence of sites across eukaryotes. As many sites are still to be discovered, this is a considerable underestimate, yet, assuming that most co‐evolving PTMs are functionally associated, we found that PTM types are vastly interconnected, forming a global network that comprise in human alone >50 000 residues in about 6000 proteins. We predict substantial PTM type interplay in secreted and membrane‐associated proteins and in the context of particular protein domains and short‐linear motifs. The global network of co‐evolving PTM types implies a complex and intertwined post‐translational regulation landscape that is likely to regulate multiple functional states of many if not all eukaryotic proteins.
This study is the first large‐scale comparative analysis of multiple types of post‐translational modifications in different eukaryotic species. The resulting network of co‐evolving and functionally associated modifications reveals the global landscape of post‐translational regulation.
Synopsis
This study is the first large‐scale comparative analysis of multiple types of post‐translational modifications in different eukaryotic species. The resulting network of co‐evolving and functionally associated modifications reveals the global landscape of post‐translational regulation.
In all, 115 149 non‐redundant post‐translational modifications (PTMs) of 13 different types were collected from 8 eukaryotes.
Comparison of evolution speed reveals that carboxylation is the most conserved while SUMOylation is the fastest evolving PTM type.
Co‐evolution of PTM pairs that co‐occur within proteins reveals a vastly interconnected global network of functionally associated PTM types in eukaryotes.
Central to the network of functionally associated PTM types appear phosphorylation, acetylation, ubiquitination and O‐linked glycosylation that control both temporal events and processes that govern protein localization.
Publisher
Nature Publishing Group UK,John Wiley & Sons, Ltd,EMBO Press,Nature Publishing Group,Springer Nature
