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pubmed:abstractText |
Plant photoreceptors regulate various developmental processes. Among the photoreceptors, phytochromes, red and far-red light receptors, regulate light responses through many signaling components, including phytochrome-interacting proteins. The functional relationships among phytochromes and their interacting proteins, however, have not been clearly established. Here, we sought to identify a functional relationship between phytochromes and phytochrome interacting factor 3 (PIF3). We demonstrate that PIF3 is polyubiquitinated rapidly and subsequently degraded in PHYA and PHYB-mediated light signaling. We also show that the degradation of PIF3 is mediated by the 26S proteasome. Our data indicate that light-stimulated phytochromes cause the degradation of their interacting protein, PIF3, by the 26S proteasome.
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