Plant receptor kinases bind and phosphorylate 14-3-3 proteins

详细信息    查看全文

• 作者：Won Byoung Chae ; Youn-Je Park ; Kyung Sun Lee ; Ill-Sup Nou ; Man-Ho Oh
• 关键词：14 ; 3 ; 3 protein ; Leucine ; rich repeat receptor ; like kinase ; BRASSINOSTEROID INSENSITIVE 1 ; Brassinosteroid ; BRI1 ; associated receptor kinase 1
• 刊名：Genes & Genomics
• 出版年：2016
• 出版时间：November 2016
• 年：2016
• 卷：38
• 期：11
• 页码：1111-1119
• 全文大小：912 KB
• 刊物主题：Microbial Genetics and Genomics; Plant Genetics & Genomics; Animal Genetics and Genomics; Human Genetics;
• 出版者：Springer Netherlands
• ISSN：2092-9293
• 卷排序：38

文摘

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.