Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C phosphatases |
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Authors: | Soon Fen-Fen Ng Ley-Moy Zhou X Edward West Graham M Kovach Amanda Tan M H Eileen Suino-Powell Kelly M He Yuanzheng Xu Yong Chalmers Michael J Brunzelle Joseph S Zhang Huiming Yang Huaiyu Jiang Hualiang Li Jun Yong Eu-Leong Cutler Sean Zhu Jian-Kang Griffin Patrick R Melcher Karsten Xu H Eric |
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Institution: | Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue NE, Grand Rapids, MI 49503, USA. |
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Abstract: | 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. |
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