Plant phosphopeptide-binding proteins as signaling mediators.
Regulation of the activity, location, and interactions of proteins by phosphorylation is crucial for many cellular processes including regulation of signaling. Phosphorylation-dependent interactions between proteins are one outcome of phosphorylation that can contribute to that regulation. Several kinds of phosphopeptide-binding proteins have been characterized, but in plants only by the forkhead-associated (FHA) domain proteins and, predominantly, the 14-3-3 proteins exist. 14-3-3 proteins have been shown to interact with several different classes of phosphorylated target proteins throughout eukaryotes. Initially, plant 14-3-3s were thought to be primarily associated with metabolic enzyme regulation; however, recent years have seen an increasing number of reports describing roles of 14-3-3 proteins in signal transduction, with plant 14-3-3 proteins now shown to interact with key proteins in signaling pathways.
Gökirmak
Tufan
T
Program in Plant Molecular and Cellular Biology, Department of Horticultural Sciences, University of Florida, Gainesville, FL 32611-0690, USA.
Paul
Anna-Lisa
AL
Ferl
Robert J
RJ
D048948:14-3-3 Proteins / Q000378:metabolism*; D008027:Light; D010748:Phosphopeptides / Q000378:metabolism*; D010766:Phosphorylation; D010937:Plant Growth Regulators / Q000378:metabolism; D018521:Plant Physiological Phenomena; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000378:metabolism / Q000528:radiation effects; D011485:Protein Binding; D015398:Signal Transduction; D013312:Stress, Physiological
D048948:14-3-3 Proteins; D010748:Phosphopeptides; D010937:Plant Growth Regulators; D010940:Plant Proteins