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KMID : 0381120160380111111
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Genes and Genomics
2016 Volume.38 No. 11 p.1111 ~ p.1119
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Plant receptor kinases bind and phosphorylate 14-3-3 proteins
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Chae Won-Byoung
Park Youn-Je
Lee Kyung-Sun
Nou Ill-Sup
Oh Man-Ho
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Abstract
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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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KEYWORD
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14-3-3 protein, Leucine-rich repeat receptor-like kinase, BRASSINOSTEROID INSENSITIVE 1, Brassinosteroid, BRI1-associated receptor kinase 1
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