Abstract
14-3-3 proteins bind to and modulate the activity of phosphorylated proteins that regulate a variety of metabolic processes in eukaryotes. Multiple 14-3-3 isoforms are expressed in most organisms and display redundancy in both sequence and function. Plants contain the largest number of 14-3-3 isoforms. For example, Arabidopsis thaliana contains thirteen 14-3-3 genes, each of which is expressed. Interest in the plant 14-3-3 field has swelled over the past decade, largely due to the vast number of possibilities for 14-3-3 metabolic regulation. As the field progresses, it is essential to understand these proteins' activities at both the spatiotemporal and subcellular levels. This review summarizes current knowledge of 14-3-3 proteins in plants, including 14-3-3 interactions, regulatory functions, isoform specificity, and post-translational modifications. We begin with a historical overview and structural analysis of 14-3-3 proteins, which describes the basic principles of 14-3-3 function, and then discuss interactions and regulatory effects of plant 14-3-3 proteins in specific tissues and subcellular compartments. We conclude with a summary of 14-3-3 phosphorylation and current knowledge of the functional effects of this modification in plants.
Highlights
The 14-3-3 proteins exist in all eukaryotes and regulate protein function generally through a direct association with phosphorylated proteins
Plants contain the largest number of 14-3-3 gene paralogs, which increases the combinatorial possibilities for specialized roles
Plants have developed fine-tuned mechanisms for cellular control through protein-protein interactions. 14-3-3 proteins are capable of influencing their binding partners in various ways, including their subcellular localization and enzymatic activities, which can vary in different organs, from primary metabolism to phototropism
Summary
The 14-3-3 proteins exist in all eukaryotes and regulate protein function generally through a direct association with phosphorylated proteins. These small, acidic proteins can function as homoor hetero-dimers, and each monomer is capable of interacting with phosphorylated serine or threonine residues of binding partners. This structural characteristic allows 14-3-3 proteins to act as scaffolding molecules during signal transduction events, bringing two phosphoproteins within close proximity of one another. Disruption of the two 14-3-3 genes (BMH1, BMH2) in yeast was reported to be lethal, but the introduction of an Arabidopsis 143-3 protein rescued this phenotype (van Heusden et al, 1995), suggesting a conserved functional role between plant and fungal 14-3-3 proteins
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