14-3-3 Proteins Participate in Light Signaling through Association with PHYTOCHROME INTERACTING FACTORs
Abstract14-3-3 proteins are regulatory proteins found in all eukaryotes and are known to selectively interact with phosphorylated proteins to regulate physiological processes. Through an affinity purification screening, many light-related proteins were recovered as 14-3-3 candidate binding partners. Yeast two-hybrid analysis revealed that the 14-3-3 kappa isoform (14-3-3κ) could bind to PHYTOCHROME INTERACTING FACTOR3 (PIF3) and CONSTITUTIVE PHOTOMORPHOGENIC1 (COP1). Further analysis by in vitro pull-down assay confirmed the interaction between 14-3-3κ and PIF3. Interruption of putative phosphorylation sites on the 14-3-3 binding motifs of PIF3 was not sufficient to inhibit 14-3-3κ from binding or to disturb nuclear localization of PIF3. It was also indicated that 14-3-3κ could bind to other members of the PIF family, such as PIF1 and PIF6, but not to LONG HYPOCOTYL IN FAR-RED1 (HFR1). 14-3-3 mutants, as well as the PIF3 overexpressor, displayed longer hypocotyls, and a pif3 mutant displayed shorter hypocotyls than the wild-type in red light, suggesting that 14-3-3 proteins are positive regulators of photomorphogenesis and function antagonistically with PIF3. Consequently, our results indicate that 14-3-3 proteins bind to PIFs and initiate photomorphogenesis in response to a light signal. View Full-Text
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Adams, E.; Diaz, C.; Hong, J.-P.; Shin, R. 14-3-3 Proteins Participate in Light Signaling through Association with PHYTOCHROME INTERACTING FACTORs. Int. J. Mol. Sci. 2014, 15, 22801-22814.
Adams E, Diaz C, Hong J-P, Shin R. 14-3-3 Proteins Participate in Light Signaling through Association with PHYTOCHROME INTERACTING FACTORs. International Journal of Molecular Sciences. 2014; 15(12):22801-22814.Chicago/Turabian Style
Adams, Eri; Diaz, Celine; Hong, Jong-Pil; Shin, Ryoung. 2014. "14-3-3 Proteins Participate in Light Signaling through Association with PHYTOCHROME INTERACTING FACTORs." Int. J. Mol. Sci. 15, no. 12: 22801-22814.