@article{168406,
  keywords = {Models, Molecular, Crystallography, X-Ray, Protein Structure, Tertiary, phosphorylation, signal transduction, Molecular Sequence Data, Protein Kinases, Amino Acid Sequence, Enzyme Activation, Arabidopsis, Sequence Deletion, Arabidopsis Proteins, Phosphoprotein Phosphatases, Abscisic Acid},
  author = {Tian Xie and Ruobing Ren and Yuan-yuan Zhang and Yuxuan Pang and Chuangye Yan and Xinqi Gong and Yuan He and Wenqi Li and Di Miao and Qi Hao and Haiteng Deng and Zhixin Wang and Jia-Wei Wu and Nieng Yan},
  title = {Molecular mechanism for inhibition of a critical component in the Arabidopsis thaliana abscisic acid signal transduction pathways, SnRK2.6, by protein phosphatase ABI1},
  abstract = {<p>Subclass III SnRK2s (SnRK2.6/2.3/2.2) are the key positive regulators of abscisic acid (ABA) signal transduction in Arabidopsis thaliana. The kinases, activated by ABA or osmotic stress, phosphorylate stress-related transcription factors and ion channels, which ultimately leads to the protection of plants from dehydration or high salinity. In the absence of stressors, SnRK2s are subject to negative regulation by group A protein phosphatase type 2Cs (PP2C), whereas the underlying molecular mechanism remains to be elucidated. Here we report the crystal structure of the kinase domain of SnRK2.6 at 2.6-{\r A} resolution. Structure-guided biochemical analyses identified two distinct interfaces between SnRK2.6 and ABI1, a member of group A PP2Cs. Structural modeling suggested that the two interfaces lock SnRK2.6 and ABI1 in an orientation such that the activation loop of SnRK2.6 is posited to the catalytic site of ABI1 for dephosphorylation. These studies revealed the molecular basis for PP2Cs-mediated inhibition of SnRK2s and provided important insights into the downstream signal transduction of ABA.</p>
},
  year = {2012},
  journal = {J Biol Chem},
  volume = {287},
  pages = {794-802},
  month = {01/2012},
  issn = {1083-351X},
  doi = {10.1074/jbc.M111.313106},
  language = {eng},
}