Activation of Arabidopsis MAPK kinase kinase (AtMEKK1) and induction of AtMEKK1-AtMEK1 pathway by wounding
Activation of Arabidopsis MAPK kinase kinase (AtMEKK1) and induction of AtMEKK1-AtMEK1 pathway by wounding
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DOI：
10.1007/s00425-005-0126-7
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发表时间：
2006-03-01
期刊：
影响因子：
4.3
通讯作者：
Yasuda, T
中科院分区：
文献类型：
--
作者：
Hadiarto, T;Nanmori, T;Yasuda, T
我们构建了一系列拟南芥MAPK激酶激酶（AtMEKK1）缺失突变体，获得了一个组成型活性突变体At-MEKK1 Delta 166，该突变体缺乏N端166个氨基酸的自抑制序列，但仍具有底物特异性。 AtMEKK1 Delta 166 主要磷酸化 AtMEK1（一种拟南芥 MAPKK），但不磷酸化其双突变体 (AtMEKIT218A/S224E)，表明 Thr-218 和 Ser-224 是磷酸化位点。在受伤的幼苗中，AtMEKK1 被激活并磷酸化其下游 AtMEK1。此外，使用抗 AtMEKK1 和抗 AtMEK1 抗体的分析表明，两种蛋白质之间的相互作用是信号依赖性的。这些结果表明存在由受伤诱导的 AtMEKK1-AtMEK1 通路。
We have constructed a series of deletion mutants of Arabidopsis MAPK kinase kinase (AtMEKK1) and obtained a constitutively active mutant, At-MEKK1 Delta 166, which lacks in self-inhibitory sequence of N-terminal 166 amino acids but still has substrate specificity. AtMEKK1 Delta 166 predominantly phosphorylates AtMEK1, an Arabidopsis MAPKK, but not its double mutant (AtMEKIT218A/S224E), suggesting that Thr-218 and Ser-224 are the phosphorylation sites. In wounded seedlings, AtMEKK1 was activated and phosphorylated its downstream AtMEK1. Furthermore, analysis using anti-AtMEKK1 and anti-AtMEK1 antibodies revealed that the interaction between the two proteins was signal dependent. These results suggest the presence of AtMEKK1-AtMEK1 pathway induced by wounding.