Location: Plant Genetics ResearchTitle: Convergent signaling pathways – interaction between methionine oxidation and serine/threonine/tyrosine O-phosphorylation
|RAO, SHYAMA PRASAD - University Of Missouri|
|MOLLER, IAN MAX - Aarhus University|
|THELEN, JAY - University Of Missouri|
Submitted to: Cell Stress and Chaperones
Publication Type: Review Article
Publication Acceptance Date: 9/10/2014
Publication Date: 9/20/2014
Publication URL: http://handle.nal.usda.gov/10113/60042
Citation: Rao, S.R., Moller, I., Thelen, J.J., Miernyk, J.A. 2014. Convergent signaling pathways – interaction between methionine oxidation and serine/threonine/tyrosine O-phosphorylation. Cell Stress and Chaperones. 20:15-21.
Interpretive Summary: Post-translational chemical modification are critically important as a component of information perception and signaling, as well as in direct control of activity, assembly, and interactions among proteins. Many chemical modifications are reversible, a property essential for roles in signaling and regulation. Recently there has been an increased appreciation for interactions or "cross-talk" between and among chemical modifications. We briefly describe the direct roles of chemical modification of Methionine (oxidation) and serine/threonine/tyrosine (O-phosphorylation), and several instances of cross-talk between the modifications. This information has the potential to help with a detailed understanding of metabolism, growth and development, and reproduction. In terms of crop plants such as soybeans, there is the potential that our understanding of this chemical modification will allow the development of lines with greater yields or custom-designed composition. The information will be most useful to to other scientists, including breeders and those using a biotech-approach to modifying seed composition.
Technical Abstract: Oxidation of Methionine (Met) to Met sulfoxide (MetSO) is a frequently found reversible post-translational 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.