Variation in Membrane Trafficking Linked to SNARE AtSYP51 Interaction With Aquaporin NIP1;1
Variation in Membrane Trafficking Linked to SNARE AtSYP51 Interaction With Aquaporin NIP1;1
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DOI：
10.3389/fpls.2018.01949
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发表时间：
2019-01-09
影响因子：
5.6
通讯作者：
Di Sansebastiano, Gian-Pietro
中科院分区：
文献类型：
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作者：
Barozzi, Fabrizio;Papadia, Paride;Di Sansebastiano, Gian-Pietro
SYP 51和SYP 52是拟南芥SYP 5 Qc-SNARE基因家族的两个成员。这两种蛋白质，除了它们的高水平的序列同一性（85%），已被证明具有不同的功能特异性，并具有不同的相互作用。在这里，我们描述了一个独特的和具体的相互作用SYP 51与ER水通道蛋白，AtNIP 1; 1（也称为NLM 1）表明能够运输亚砷酸盐[As（III）]和以前本地化PM。在目前的工作中，我们详细研究了这种定位在体内和表征与SYP 51的相互作用。我们认为，这种相互作用可能揭示了一个新的机制，调节液泡膜内陷和回收。我们建议这种相互作用的一部分，直接从内质网到液泡膜和高尔基体介导的小泡运输的膜运输相关的监管机制。我们还表明，NIP 1;1是重要的植物耐受亚砷酸盐，但不改变其吸收或转运。为了解释这一现象的假说，SYP 51/NIP 1;1相互作用修改ER和液泡积累亚砷酸盐的能力进行了讨论。
SYP51 and 52 are the two members of the SYP5 Qc-SNARE gene family in Arabidopsis thaliana. These two proteins, besides their high level of sequence identity (85%), have shown to have differential functional specificity and possess a different interactome. Here we describe a unique and specific interaction of SYP51 with an ER aquaporin, AtNIP1; 1 (also known as NLM 1) indicated to be able to transport arsenite [As(III)] and previously localized on PM. In the present work we investigate in detail such localization in vivo and characterize the interaction with SYP51. We suggest that this interaction may reveal a new mechanism regulating tonoplast invagination and recycling. We propose this interaction to be part of a regulatory mechanism associated with direct membrane transport from ER to tonoplast and Golgi mediated vesicle trafficking. We also demonstrate that NIP1;1 is important for plant tolerance to arsenite but does not alter its uptake or translocation. To explain such phenomenon the hypothesis that SYP51/NIP1;1 interaction modifies ER and vacuole ability to accumulate arsenite is discussed.