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首页> 外文期刊>Molecular & cellular proteomics: MCP >Multiple phosphorylations in the C-terminal tail of plant plasma membrane aquaporins: role in subcellular trafficking of AtPIP2;1 in response to salt stress.
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Multiple phosphorylations in the C-terminal tail of plant plasma membrane aquaporins: role in subcellular trafficking of AtPIP2;1 in response to salt stress.

机译：植物质膜水通道蛋白C末端尾部的多个磷酸化：在AtPIP2; 1响应盐胁迫的亚细胞运输中的作用。

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摘要

Aquaporins form a family of water and solute channel proteins and are present in most living organisms. In plants, aquaporins play an important role in the regulation of root water transport in response to abiotic stresses. In this work, we investigated the role of phosphorylation of plasma membrane intrinsic protein (PIP) aquaporins in the Arabidopsis thaliana root by a combination of quantitative mass spectrometry and cellular biology approaches. A novel phosphoproteomics procedure that involves plasma membrane purification, phosphopeptide enrichment with TiO(2) columns, and systematic mass spectrometry sequencing revealed multiple and adjacent phosphorylation sites in the C-terminal tail of several AtPIPs. Six of these sites had not been described previously. The phosphorylation of AtPIP2;1 at two C-terminal sites (Ser(280) and Ser(283)) was monitored by an absolute quantification method and shown to be altered in response to treatments of plants by salt (NaCl) and hydrogen peroxide. The two treatments are known to strongly decrease the water permeability of Arabidopsis roots. To investigate a putative role of Ser(280) and Ser(283) phosphorylation in aquaporin subcellular trafficking, AtPIP2;1 forms mutated at either one of the two sites were fused to the green fluorescent protein and expressed in transgenic plants. Confocal microscopy analysis of these plants revealed that, in resting conditions, phosphorylation of Ser(283) is necessary to target AtPIP2;1 to the plasma membrane. In addition, an NaCl treatment induced an intracellular accumulation of AtPIP2;1 by exerting specific actions onto AtPIP2;1 forms differing in their phosphorylation at Ser(283) to induce their accumulation in distinct intracellular structures. Thus, the present study documents stress-induced quantitative changes in aquaporin phosphorylation and establishes for the first time a link with plant aquaporin subcellular localization.
机译：水通道蛋白形成水和溶质通道蛋白家族，并存在于大多数活生物体中。在植物中，水通道蛋白在响应非生物胁迫而调节根水运输中起重要作用。在这项工作中，我们通过定量质谱和细胞生物学方法的结合，研究了拟南芥根中质膜内在蛋白（PIP）水通道蛋白的磷酸化作用。一种新颖的磷酸化蛋白质组学程序，涉及质膜纯化，磷酸肽与TiO（2）柱富集和系统的质谱测序，揭示了多个AtPIP的C末端尾巴中的多个和相邻的磷酸化位点。这些站点中有六个以前没有描述过。通过绝对定量方法监测两个C末端位点（Ser（280）和Ser（283））AtPIP2; 1的磷酸化，并显示响应于盐（NaCl）和过氧化氢处理植物而发生了改变。已知这两种处理会大大降低拟南芥根的透水性。为了研究在水通道蛋白亚细胞运输中Ser（280）和Ser（283）磷酸化的推定作用，将在两个位点之一突变的AtPIP2; 1形式与绿色荧光蛋白融合并在转基因植物中表达。这些植物的共聚焦显微镜分析表明，在静止条件下，Ser（283）的磷酸化对于将AtPIP2; 1靶向质膜是必要的。此外，NaCl处理通过对AtPIP2; 1形式施加不同的作用以诱导其在Ser（283）处的磷酸化，从而诱导AtPIP2; 1的细胞内积累，从而诱导其在不同的细胞内结构中积累。因此，本研究记录了胁迫诱导的水通道蛋白磷酸化的定量变化，并首次建立了与植物水通道蛋白亚细胞定位的联系。

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