Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C phosphatases.

Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C phosphatases.
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DOI:
10.1126/science.1215106
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发表时间:
2012-01-06
期刊:
Science (New York, N.Y.)
影响因子:
--
通讯作者:
Xu HE
Xu HE
中科院分区:
其他
文献类型:
--
作者:
Soon FF;Ng LM;Zhou XE;West GM;Kovach A;Tan MH;Suino-Powell KM;He Y;Xu Y;Chalmers MJ;Brunzelle JS;Zhang H;Yang H;Jiang H;Li J;Yong EL;Cutler S;Zhu JK;Griffin PR;Melcher K;Xu HE

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脱落酸(阿坝)是植物在逆境中生存所必需的激素。在阿坝信号传导网络的中心是2C型蛋白磷酸酶(PP 2C)的亚家族,其与阿坝受体和亚家族2 Snfl相关激酶(SnRK 2)形成排他性相互作用。在这里,我们报告了SnRK 2-PP 2C复合物的结构,揭示了SnRK 2和阿坝受体识别PP 2C的显着相似性。在复合物中,激酶活化环对接到PP 2C的活性位点,而PP 2C的保守ABA敏感色氨酸插入到激酶催化裂缝中,从而模拟受体-PP 2C相互作用。这些结构的结果提供了一个简单的机制,直接耦合阿坝结合SnRK 2激酶激活,并强调了一个新的范例,通过相互包装的催化位点的激酶磷酸酶调节。
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.
脱甲酸受体的激素信号传导的栅极锁锁机制。
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