Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C phosphatases

Fen Fen Soon, Ley Moy Ng, X. Edward Zhou, Graham M. West, Amanda Kovach, M. H.Eileen Tan, Kelly M. Suino-Powell, Yuanzheng He, Yong Xu, Michael J. Chalmers, Joseph S. Brunzelle, Huiming Zhang, Huaiyu Yang, Hualiang Jiang, Jun Li, Eu Leong Yong, Sean Cutler, Jian Kang Zhu, Patrick R. Griffin, Karsten Melcher*H. Eric Xu

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

268 Scopus citations


Abscisic acid (ABA) is an essential hormone for plants to survive environmental stresses. At the center of the ABA signaling network is a subfamily of type 2C protein phosphatases (PP2Cs), which form exclusive interactions with ABA receptors and subfamily 2 Snfl-related kinase (SnRK2s). Here, we report a SnRK2-PP2C complex structure, which reveals marked similarity in PP2C recognition by SnRK2 and ABA receptors. In the complex, the kinase activation loop docks into the active site of PP2C, while the conserved ABA-sensing tryptophan of PP2C inserts into the kinase catalytic cleft, thus mimicking receptor-PP2C interactions. These structural results provide a simple mechanism that directly couples ABA binding to SnRK2 kinase activation and highlight a new paradigm of kinase-phosphatase regulation through mutual packing of their catalytic sites.

Original languageEnglish (US)
Pages (from-to)85-88
Number of pages4
Issue number6064
StatePublished - Jan 6 2012

ASJC Scopus subject areas

  • General


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