Interplay of Metal Ions and Posttranslational Modifications in Proteins

Abstract

Posttranslational modifications (PTMs) and metal ions are integral players in the complex regulatory orchestra governing protein function. Several metal ions, including zinc, iron, copper, and others, intricately influence protein structure and activity as cofactors. Concurrently, PTMs, such as phosphorylation, acetylation, and ubiquitination, add an additional layer of complexity to the proteome, dynamically shaping cellular responses. Understanding this bidirectional relationship is crucial for unraveling the complex web of cellular regulation. This review explores the reciprocal impact of metal ions on PTMs and vice versa and provides examples and insights into how metal ions modulate PTMs and, conversely, how PTMs influence metal-binding proteins, shedding light on the complex crosstalk between these two crucial facets of cellular biology. This interplay is not only central to cellular homeostasis but also holds implications for diseases associated with dysregulated metal-ion and PTM processes.