title: Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C phosphatases.
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.
authors: Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue NE, Grand Rapids, MI 49503, USA.
authors: Fen-Fen
authors: FF
authors: Soon
authors: Ley-Moy
authors: LM
authors: Ng
authors: X Edward
authors: XE
authors: Zhou
authors: Graham M
authors: GM
authors: West
authors: Amanda
authors: A
authors: Kovach
authors: M H Eileen
authors: MH
authors: Tan
authors: Kelly M
authors: KM
authors: Suino-Powell
authors: Yuanzheng
authors: Y
authors: He
authors: Yong
authors: Y
authors: Xu
authors: Michael J
authors: MJ
authors: Chalmers
authors: Joseph S
authors: JS
authors: Brunzelle
authors: Huiming
authors: H
authors: Zhang
authors: Huaiyu
authors: H
authors: Yang
authors: Hualiang
authors: H
authors: Jiang
authors: Jun
authors: J
authors: Li
authors: Eu-Leong
authors: EL
authors: Yong
authors: Sean
authors: S
authors: Cutler
authors: Jian-Kang
authors: JK
authors: Zhu
authors: Patrick R
authors: PR
authors: Griffin
authors: Karsten
authors: K
authors: Melcher
authors: H Eric
authors: HE
authors: Xu
mesh_terms: D000040:Abscisic Acid / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000737:chemistry / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004789:Enzyme Activation; D008958:Models, Molecular; D018716:Molecular Mimicry; D008969:Molecular Sequence Data; D010749:Phosphoprotein Phosphatases / Q000737:chemistry* / Q000378:metabolism*; D010766:Phosphorylation; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D029681:Arabidopsis Proteins; C569327:PYL2 protein, Arabidopsis; D011993:Recombinant Fusion Proteins; C492978:SnRK2 protein, Arabidopsis; D000040:Abscisic Acid; D017346:Protein Serine-Threonine Kinases; C106443:ABI2 protein, Arabidopsis; C514757:HAB1 protein, Arabidopsis; D010749:Phosphoprotein Phosphatases