N-Myristoylation in Plants: Molecular Mechanisms, Protein Fate, and Roles in Stress Responses and Development

N-myristoylation is a common yet poorly understood protein lipid modification in all eukaryotes, including plants. It involves the covalent attachment of myristic acid to the N-terminal glycine of target proteins, catalyzed by N-myristoyltransferase. This modification can alter the structure and membrane anchoring of target proteins, thereby playing a significant role in regulating protein fate, including subcellular compartmentalization and stability. Currently, increasing evidence has highlighted the vital role of N-myristoylation in regulating plant immunity, abiotic stress responses, growth, and development, underscoring its biological significance for plant environmental adaptation and survival. Despite its importance, the fundamental mechanisms of N-myristoylation and its specific regulatory effects on plant protein function and fate remain incompletely characterized. In this review, we first summarize the core biochemical process of protein N-myristoylation and the functional features of its catalytic enzyme, N-myristoyltransferase. We then elaborate on the molecular basis by which this modification modulates protein fate, before providing a comprehensive overview of its diverse biological functions in the aforementioned plant physiological processes. Additionally, we critically evaluate major technical approaches for detecting N-myristoylation, clarifying their respective advantages and inherent limitations. Finally, we propose promising future directions, aiming to provide a theoretical foundation for subsequent investigations in this rapidly developing field.