EHD1 functions in endosomal recycling and confers salt tolerance.

EHD1 functions in endosomal recycling and confers salt tolerance.
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DOI:
10.1371/journal.pone.0054533
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发表时间:
2013
期刊:
影响因子:
3.7
通讯作者:
Avni A
Avni A
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Bar M;Leibman M;Schuster S;Pitzhadza H;Avni A

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内吞作用是包括植物在内的所有真核生物的重要过程。我们以前已经表明,两个拟南芥蛋白,AtEHD 1和AtEHD 2,参与植物系统中的内吞作用。敲低EHD 1显示出在马里亚人中具有延迟再循环表型。在哺乳动物系统中有许多工作详细说明了EHD中各个结构域的重要性,但迄今为止,植物EHD 1的活性所需的结构域尚未被表征。在这项工作中,我们证明,敲低EHD 1导致延迟再循环表型,并降低布雷菲德菌素A的敏感性在拟南芥幼苗。EHD 1的EH结构域被发现对于EHD 1定位于内体结构至关重要。缺乏EH结构域的突变体EHD 1没有定位于内体结构,并表现出与EHD 1敲除幼苗相似的表型。然而,缺乏卷曲螺旋结构域的突变体表现出与野生型或EHD 1过表达幼苗相似的表型。盐胁迫是当前农业面临的主要问题。微阵列数据表明,盐胁迫增强EHD 1的表达,这是证实了半定量RT-PCR。我们在此证明,过表达EHD 1的转基因植物具有增强的耐盐性,这也需要一个完整的EH结构域的属性。
Endocytosis is a crucial process in all eukaryotic organisms including plants. We have previously shown that two Arabidopsis proteins, AtEHD1 and AtEHD2, are involved in endocytosis in plant systems. Knock-down of EHD1 was shown to have a delayed recycling phenotype in mammalians. There are many works in mammalian systems detailing the importance of the various domains in EHDs but, to date, the domains of plant EHD1 that are required for its activity have not been characterized. In this work we demonstrate that knock-down of EHD1 causes a delayed recycling phenotype and reduces Brefeldin A sensitivity in Arabidopsis seedlings. The EH domain of EHD1 was found to be crucial for the localization of EHD1 to endosomal structures. Mutant EHD1 lacking the EH domain did not localize to endosomal structures and showed a phenotype similar to that of EHD1 knock-down seedlings. Mutants lacking the coiled-coil domain, however, showed a phenotype similar to wild-type or EHD1 overexpression seedlings. Salinity stress is a major problem in current agriculture. Microarray data demonstrated that salinity stress enhances the expression of EHD1, and this was confirmed by semi quantitative RT-PCR. We demonstrate herein that transgenic plants over expressing EHD1 possess enhanced tolerance to salt stress, a property which also requires an intact EH domain.
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