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首页> 外文期刊>Neuron >Regulation of DLK-1 Kinase Activity by Calcium-Mediated Dissociation from an Inhibitory Isoform
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Regulation of DLK-1 Kinase Activity by Calcium-Mediated Dissociation from an Inhibitory Isoform

机译：钙介导的解离抑制同工型对DLK-1激酶活性的调节。

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MAPKKK dual leucine zipper-bearing kinases (DLKs) are regulators of synaptic development and axon regeneration. The mechanisms underlying their activation are not fully understood. Here, we show that C. elegans DLK-1 is activated by a Ca 2+-dependent switch from inactive heteromeric to active homomeric protein complexes. We identify a DLK-1 isoform, DLK-1S, that shares identical kinase and leucine zipper domains with the previously described long isoform DLK-1L but acts to inhibit DLK-1 function by binding to DLK-1L. The switch between homo- or heteromeric DLK-1 complexes is influenced by Ca 2+ concentration. A conserved hexapeptide in the DLK-1L C terminus is essential for DLK-1 activity and is required for Ca 2+ regulation. The mammalian DLK-1 homolog MAP3K13 contains an identical C-terminal hexapeptide and can functionally complement dlk-1 mutants, suggesting that the DLK activation mechanism is conserved. The DLK activation mechanism is ideally suited for rapid and spatially controlled signal transduction in response to axonal injury and synaptic activity. MAPKKK dual leucine zipper-bearing kinases (DLKs) are regulators of synaptic development and axon regeneration. Yan and Jin show that C. elegans DLK-1 is activated by a Ca 2+-dependent switch from inactive heteromeric to active homomeric protein complexes.
机译：MAPKKK双亮氨酸拉链激酶（DLKs）是突触发育和轴突再生的调节剂。其激活的机制尚不完全清楚。在这里，我们显示秀丽隐杆线虫DLK-1是由Ca 2+依赖性开关激活的，该开关从无活性的异聚体转变为有活性的同聚体蛋白复合物。我们确定了一个DLK-1亚型，DLK-1S，与先前描述的长亚型DLK-1L共享相同的激酶和亮氨酸拉链结构域，但通过与DLK-1L结合来抑制DLK-1的功能。同源或异源DLK-1复合物之间的转换受Ca 2+浓度影响。 DLK-1L C末端的保守六肽对于DLK-1活性至关重要，也是调节Ca 2+所必需的。哺乳动物的DLK-1同源物MAP3K13包含相同的C端六肽，可以在功能上与dlk-1突变体互补，这表明DLK激活机制是保守的。 DLK激活机制非常适合响应轴突损伤和突触活动的快速和空间控制的信号转导。 MAPKKK双亮氨酸拉链激酶（DLKs）是突触发育和轴突再生的调节剂。 Yan和Jin表明，秀丽隐杆线虫DLK-1被Ca 2+依赖的开关激活，该开关从无活性的异聚蛋白转变为有活性的同聚蛋白复合物。

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