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AUTHOR |
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Bong-Kwan Phee*, Jeong-Il Kim*, Dong Ho Shin, Jihye Yoo, Kyoung-Jin Park, Yun-Jeong Han, Yong-Kook Kwon, Man-Ho Cho, Jong-Seong Jeon, Seong Hee Bhoo,Tae-Ryong Hahn (2008) |
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A novel protein phosphatase indirectly regulates phytochrome interacting factor 3 via phytochrome |
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JOURNAL |
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Biochemical Journal, 415(2): 247-255 |
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The Abstract Of The Paper |
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Light signal transduction in plants involves an intricate series of pathways which is finely regulated by interactions between specific signaling proteins, as well as by protein modifications such as phosphorylation and ubiquitination. The identification of novel phytochrome-interacting proteins and the precise signaling mechanisms that they mediate is still ongoing. In our current study, we show that the newly identified putative phytochrome-associated protein, PAPP2C (phytochrome-associated protein phosphatase 2 type 2C), interacts in the nucleus with phytochrome A (phyA) and B (phyB), both in vitro and in vivo. Moreover, the phosphatase activity of PAPP2C and its association with phytochromes were found to be enhanced by red light, indicating that it plays a role in mediating phytochrome signaling. In particular, PAPP2C specifically binds to the Nterminal PHY domain of the phytochromes. We thus speculate that this interaction reflects a unique regulatory function of this phosphatase toward established phytochromeassociated proteins. We also show that PAPP2C effectively dephosphorylates phytochromes in vitro. Interestingly, PAPP2C indirectly mediates the dephosphorylation of phytochrome interacting factor 3 (PIF3) in vitro. Taken together, we suggest that PAPP2C functions as a regulator of PIF3 by dephosphorylating phytochromes in the nucleus.
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