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Updated: Sep 4, 2025

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
Published on: February 27, 2020
The evolution of post-translational modifications
1PROTEO-Regroupement québécois de recherche sur la fonction, l'ingénierie et les applications des protéines, Québec, QC, Canada; Département de biologie, Université Laval, Québec, QC, Canada; Département de biochimie, de microbiologie et de bio-informatique, Université Laval, Québec, QC, Canada; Centre de recherche en données massives de l'Université Laval, Université Laval, Québec, QC, Canada; Institut de biologie intégrative et des systèmes (IBIS), Université Laval, Québec, QC, Canada.
Abstract:
Post-translational modifications (PTMs) are chemical modifications that can regulate the activity and function of proteins. From an evolutionary perspective, they also represent a fast mechanism for the generation of phenotypic diversity and divergence. Advances in mass spectrometry have now enabled the identification of over 600 distinct PTM classes collectively spanning an order of 106 unique sites. However, the chemical detection of PTMs has lagged far behind their functional characterisation, and relatively little is still known about the selective constraints that govern PTM evolution. In particular, the true fraction of PTM sites that are functional - and thus subject to selection - remains an open question. Here, I review advances made in the past two years towards understanding the evolution of PTMs and their associated enzymes.
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