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Identification of Post-translational Modifications of Plant Protein Complexes
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Turnover of protein phosphorylation evolving under stabilizing selection.

Christian R Landry1, Luca Freschi1, Taraneh Zarin2

  • 1Département de Biologie, Université Laval Québec, QC, Canada ; Institut de Biologie Intégrative et des Systèmes (IBIS), Université Laval Québec, QC, Canada ; Network for Research on Protein Function, Structure, and Engineering (PROTEO), Univeristé Laval Québec, QC, Canada.

Frontiers in Genetics
|August 8, 2014
PubMed
Summary

Posttranslational modifications, like protein phosphorylation, regulate protein function and impact evolution and disease. This study explores two modes of phosphorylation regulation and their evolutionary implications.

Keywords:
cell signalingevolutionary turnovermolecular evolutionmolecular rheostatsmolecular switchesprotein evolutionprotein phosphorylation

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Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Molecular Biology

Background:

  • Posttranslational modifications (PTMs) regulate protein function, influencing evolution and disease.
  • Phosphorylation, a common PTM, affects protein stability, localization, and interactions.
  • The precise roles of most phosphorylation sites remain largely uncharacterized.

Purpose of the Study:

  • To discuss two distinct modes of protein phosphorylation regulation.
  • To examine how these regulatory modes influence the evolution of protein phosphorylation.
  • To explore the study of phosphorylation site clusters within the framework of complex traits evolution.

Main Methods:

  • Literature review and conceptual analysis of phosphorylation mechanisms.
  • Discussion of existing functional studies on protein phosphorylation.
  • Application of evolutionary frameworks to phosphorylation site evolution.

Main Results:

  • Two modes of phosphorylation regulation are identified: 'molecular switches' and 'rheostats'.
  • These modes differentially impact the rate and patterns of protein phosphorylation evolution.
  • Evolution of phosphorylation site clusters can be analyzed using complex traits and stabilizing selection models.

Conclusions:

  • Understanding phosphorylation modes is crucial for deciphering evolutionary dynamics.
  • The 'rheostat' mode, involving clusters of sites, offers a new perspective on protein regulation evolution.
  • Phosphorylation evolution is linked to complex traits and stabilizing selection, offering avenues for future research.