Convergent signaling pathways-interaction between methionine oxidation and serine/threonine/tyrosine O-phosphorylation

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  • R Shyama Prasad Rao, Division of Biochemistry, University of Missouri, Columbia, United States
  • Ian Max Møller
  • Jay J Thelen, Division of Biochemistry, University of Missouri, Columbia, United States
  • Ján A Miernyk, Division of Biochemistry, University of Missouri, Columbia, Plant Genetics Research Unit, USDA, Agricultural Research Service, University of Missouri, United States

Oxidation of methionine (Met) to Met sulfoxide (MetSO) is a frequently found reversible posttranslational modification. It has been presumed that the major functional role for oxidation-labile Met residues is to protect proteins/cells from oxidative stress. However, Met oxidation has been established as a key mechanism for direct regulation of a wide range of protein functions and cellular processes. Furthermore, recent reports suggest an interaction between Met oxidation and O-phosphorylation. Such interactions are a potentially direct interface between redox sensing and signaling, and cellular protein kinase/phosphatase-based signaling. Herein, we describe the current state of Met oxidation research, provide some mechanistic insight into crosstalk between these two major posttranslational modifications, and consider the evolutionary significance and regulatory potential of this crosstalk.

Original languageEnglish
JournalCell Stress & Chaperones
Pages (from-to)15-21
Number of pages7
Publication statusPublished - 2015

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