Genes & Genomics

, Volume 38, Issue 11, pp 1111–1119 | Cite as

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

  • Won Byoung Chae
  • Youn-Je Park
  • Kyung Sun Lee
  • Ill-Sup Nou
  • Man-Ho OhEmail author
Research Article


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.


14-3-3 protein Leucine-rich repeat receptor-like kinase BRASSINOSTEROID INSENSITIVE 1 Brassinosteroid BRI1-associated receptor kinase 1 



This work was supported in part by the research fund of Chungnam National University, Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (No. 2014R1A1A401006751) and Golden Seed Project (Center for Horticultural Seed Development, No. 213003-04-4-SB110 by Ministry of Agriculture, Food and Rural Affairs (MAFRA), Ministry of Oceans and Fisheries (MOF), Rural Development Administration (RDA) and Korea Forest Service (KFS). This work was carried out with the support of “Cooperative Research Program for Agriculture Science & Technology Development (Project No. PJ01024701)” by Rural Development Administration, Republic of Korea.

Compliance with ethical standards

Conflict of interest

Won Byoung Chae, Youn-Je Park, Kyung Sun Lee, Ill-Sup Nou and Man-Ho Oh declares no conflict of interest.

Studies with human or animal research

This article does not contain any studies with human subjects or animals performed by any of the authors.


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Copyright information

© The Genetics Society of Korea and Springer-Science and Media 2016

Authors and Affiliations

  • Won Byoung Chae
    • 1
  • Youn-Je Park
    • 2
  • Kyung Sun Lee
    • 3
  • Ill-Sup Nou
    • 4
  • Man-Ho Oh
    • 3
    Email author
  1. 1.Vegetable Research DivisionNational Institute of Horticultural and Herbal Science, RDAWanjuRepublic of Korea
  2. 2.Department of Food Science and TechnologyKongju National UniversiyYesanRepublic of Korea
  3. 3.Department of Biological Sciences, College of Biological Sciences and BiotechnologyChungnam National UniversityDaejeonRepublic of Korea
  4. 4.Department of HorticultureSunchon National UniversitySunchonRepublic of Korea

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