Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C phosphatases.
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.
Mesh Terms:
Abscisic Acid, Amino Acid Sequence, Arabidopsis, Arabidopsis Proteins, Catalytic Domain, Crystallography, X-Ray, Enzyme Activation, Models, Molecular, Molecular Mimicry, Molecular Sequence Data, Phosphoprotein Phosphatases, Phosphorylation, Protein Binding, Protein Structure, Tertiary, Protein-Serine-Threonine Kinases, Recombinant Fusion Proteins, Signal Transduction
Abscisic Acid, Amino Acid Sequence, Arabidopsis, Arabidopsis Proteins, Catalytic Domain, Crystallography, X-Ray, Enzyme Activation, Models, Molecular, Molecular Mimicry, Molecular Sequence Data, Phosphoprotein Phosphatases, Phosphorylation, Protein Binding, Protein Structure, Tertiary, Protein-Serine-Threonine Kinases, Recombinant Fusion Proteins, Signal Transduction
Science
Date: Jan. 06, 2012
PubMed ID: 22116026
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