Plant receptor kinases bind and phosphorylate 14-3-3 proteins |
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Authors: | Won Byoung Chae Youn-Je Park Kyung Sun Lee Ill-Sup Nou Man-Ho Oh |
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Institution: | 1.Vegetable Research Division,National Institute of Horticultural and Herbal Science, RDA,Wanju,Republic of Korea;2.Department of Food Science and Technology,Kongju National Universiy,Yesan,Republic of Korea;3.Department of Biological Sciences, College of Biological Sciences and Biotechnology,Chungnam National University,Daejeon,Republic of Korea;4.Department of Horticulture,Sunchon National University,Sunchon,Republic of Korea |
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Abstract: | 14-3-3 proteins are pSer/pThr-binding proteins that interact with a wide array of cellular ‘client’ proteins. The plant brassinosteroids (BRs) receptor, BRASSINOSTEROID INSENSITIVE 1 (BRI1), is a member of the large family of leucine-rich repeat receptor-like kinases (LRR-RLKs) that contain cytoplasmic protein kinase domains. At least two LRR-RLKs are involved in BR perception and signal transduction: BRI1 and BRI1-associated receptor kinase 1 (BAK1). We determined that several 14-3-3 proteins bind to BRI1-CD and are phosphorylated by BRI1, BAK1 and At3g21430 receptor kinases in vitro. Moreover, we observed14-3-3 s are phosphorylated on threonine residue(s) with BR-dependent manner. To reveal the function of 14-3-3 proteins interacting with LRR-RLKs, we treated tyrosine phosphatase (PTP1B) to the BRI1-CD recombinant protein, which is autophosphorylated on tyrosine residue(s). Tyrosine autophosphorylation signal was disappeared, suggesting that 14-3-3 proteins cannot protect BRI1 tyrosine phosphorylation from PTP1B phosphatase. Our study suggests that 14-3-3 proteins may be important for plant growth and development through BR signaling. |
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