Harnessing the interplay of protein posttranslational modifications: Enhancing plant resilience to heavy metal toxicity

Heavy metals (HMs) toxicity finds substantial plant health risk, affecting germination, growth, productivity, and survival. HMs exposure can interrupt cellular function, increase oxidative stress and affect physiological processes. Plants have developed array of adaptive responses, with proteins playing key role in detecting, signalling, and mitigating metal-induced stress. Under stress, posttranslational modifications, including phosphorylation, ubiquitination, glycosylation and acetylation, are essential regulators of protein stability, localization, and function. This review examines the comprehensive profiling of PTMs in HMs stress responses, including how PTMs regulate the signalling pathways, degradation pathways, and TFs modulation. Specifically, discuss the role of phosphorylation, ubiquitination, and sumoylation, neddylation, lipidation, and S-nitrosylation in specifically under HMs stress with PTMs regulation of antioxidant enzymes, stress proteins, metal transporters and chelators of detoxification. This review illustrates the crosstalk of PTMs to show how synergistic interactions regulate protein stability, activity, and localization upon HMs stress. In cross talk, ubiquitination often starts from phosphorylation to subsequent degradation of proteins in a timely and reversible way to trigger stress responses. However, sumoylation stabilizes key transcription factors that are rapidly dephosphorylated and integral in metal detoxification, form a synergistic combination with phosphorylation to maintain their activity. It explains the future research directions, focusing on PTM engineering to generate stress tolerant plant varieties. By studying the response of plants to HMs stress through PTMs, emphasizes the relevance of PTMs towards plant resilience and advocates for systems biology integrative approach to advancing plant stress biology.