Phosphatidic Acid Regulates Microtubule Organization by Interacting with MAP65-1 in Response to Salt Stress in Arabidopsis
Phosphatidic Acid Regulates Microtubule Organization by Interacting with MAP65-1 in Response to Salt Stress in Arabidopsis
复制标题
拟南芥中磷脂酸通过与 MAP65-1 相互作用来调节微管组织以响应盐胁迫
DOI：
10.1105/tpc.112.104182
复制
发表时间：
2012-11-01
期刊：
影响因子：
11.6
通讯作者：
Zhang, Wenhua
中科院分区：
文献类型：
--
作者：
Zhang, Qun;Lin, Feng;Zhang, Wenhua
膜脂在细胞代谢和信号转导中起着基本的结构和调节作用。在这里，我们报告磷脂酸（PA），磷脂酶D（PLD）的产物，调节微管相关蛋白MAP 65 -1，在盐胁迫的反应。PLD α 1基因的敲除导致更大的NaCl诱导的微管的解体，这不能恢复期间或之后去除的压力。盐可影响微管与MAP 65 -1的结合，导致pld α 1细胞微管结构紊乱，外源性PA可减轻这种紊乱。PA与MAP 65 -1结合，增加其增强微管聚合和成束的活性。MAP 65 -1的过表达提高了拟南芥细胞的耐盐性。MAP 65 -1中8个氨基酸的突变导致其与PA结合、微管捆绑活性和耐盐性的增强的丧失。pld α 1 map 65 -1双突变体对盐胁迫的敏感性高于单突变体。这些结果表明，PLD α 1衍生的PA与MAP 65 -1结合，从而介导微管稳定和耐盐性。MAP 65 -1作为PA靶点的鉴定揭示了环境应激信号传导中膜脂和细胞骨架之间的功能联系。
Membrane lipids play fundamental structural and regulatory roles in cell metabolism and signaling. Here, we report that phosphatidic acid (PA), a product of phospholipase D (PLD), regulates MAP65-1, a microtubule-associated protein, in response to salt stress. Knockout of the PLD alpha 1 gene resulted in greater NaCl-induced disorganization of microtubules, which could not be recovered during or after removal of the stress. Salt affected the association of MAP65-1 with microtubules, leading to microtubule disorganization in pld alpha 1cells, which was alleviated by exogenous PA. PA bound to MAP65-1, increasing its activity in enhancing microtubule polymerization and bundling. Overexpression of MAP65-1 improved salt tolerance of Arabidopsis thaliana cells. Mutations of eight amino acids in MAP65-1 led to the loss of its binding to PA, microtubule-bundling activity, and promotion of salt tolerance. The pld alpha 1 map65-1 double mutant showed greater sensitivity to salt stress than did either single mutant. These results suggest that PLD alpha 1-derived PA binds to MAP65-1, thus mediating microtubule stabilization and salt tolerance. The identification of MAP65-1 as a target of PA reveals a functional connection between membrane lipids and the cytoskeleton in environmental stress signaling.