Multifaceted functions of post-translational enzyme modifications in the control of plant glycolysis

• Published in: Current opinion in plant biology Vol. 55; pp. 28 - 37
• Main Authors: O’Leary, Brendan, Plaxton, William C
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.06.2020
• ISSN: 1369-5266; 1879-0356
• DOI: 10.1016/j.pbi.2020.01.009

[Display omitted] •PTM’s and allosteric effectors interact to control glycolytic enzyme activities.•Reversible phosphorylation, redox-sensitive thiol modifications, and monoubiquitination are the most prevalent regulatory PTMs of plant glycolytic enzymes.•PEP carboxylase provides one of the most comprehensive examples of the post-translational control of plant glycolysis by allosteric effectors, PTMs, and protein:protein interactions.•Evaluating the impact and mechanisms of enzyme PTMs in the regulation and functions of plant glycolysis is a key area for future research. Glycolysis is a central feature of metabolism and its regulation plays important roles during plant developmental and stress responses. Recent advances in proteomics and mass spectrometry have documented extensive and dynamic post-translational modifications (PTMs) of most glycolytic enzymes in diverse plant tissues. Protein PTMs represent fundamental regulatory events that integrate signalling and gene expression with cellular metabolic networks, and can regulate glycolytic enzyme activity, localization, protein:protein interactions, moonlighting functions, and turnover. Serine/threonine phosphorylation and redox PTMs of cysteine thiol groups appear to be the most prevalent forms of reversible covalent modification involved in plant glycolytic control. Additional PTMs including monoubiquitination also have important functions. However, the molecular functions and mechanisms of most glycolytic enzyme PTMs remain unknown, and represent important objectives for future studies.