Abstract
In this review we highlight the advances achieved in the investigation of the role of 14-3-3 proteins in hormone signaling, biosynthesis, and transport. 14-3-3 proteins are a family of conserved molecules that target a number of protein clients through their ability to recognize well-defined phosphorylated motifs. As a result, they regulate several cellular processes, ranging from metabolism to transport, growth, development, and stress response. High-throughput proteomic data and two-hybrid screen demonstrate that 14-3-3 proteins physically interact with many protein clients involved in the biosynthesis or signaling pathways of the main plant hormones, while increasing functional evidence indicates that 14-3-3-target interactions play pivotal regulatory roles. These advances provide a framework of our understanding of plant hormone action, suggesting that 14-3-3 proteins act as hubs of a cellular web encompassing different signaling pathways, transducing and integrating diverse hormone signals in the regulation of physiological processes.
Highlights
14-3-3 proteins are highly conserved dimeric proteins with a subunit mass of 30 kDa, widespread in eukaryotic organisms (Aitken et al, 1992; Fu et al, 2000; Huber et al, 2002)
The high degree of sequence conservation among isoforms suggests a corresponding functional redundancy, increasing evidence demonstrates that 14-3-3 isoforms bind to individual targets with different affinities, thereby opening the possibility that regulation of specific processes could be accomplished by single 14-3-3 isoforms (Paul et al, 2012; Pallucca et al, 2014)
This review highlighted the involvement of 14-3-3 proteins in plant hormone regulation, an emerging topic concerning 14-33 functions
Summary
In this review we highlight the advances achieved in the investigation of the role of 14-3-3 proteins in hormone signaling, biosynthesis, and transport. 14-3-3 proteins are a family of conserved molecules that target a number of protein clients through their ability to recognize well-defined phosphorylated motifs. High-throughput proteomic data and two-hybrid screen demonstrate that 14-3-3 proteins physically interact with many protein clients involved in the biosynthesis or signaling pathways of the main plant hormones, while increasing functional evidence indicates that 14-3-3-target interactions play pivotal regulatory roles. These advances provide a framework of our understanding of plant hormone action, suggesting that 14-3-3 proteins act as hubs of a cellular web encompassing different signaling pathways, transducing and integrating diverse hormone signals in the regulation of physiological processes
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