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首页> 外文期刊>Biochimica et biophysica acta. Biomembranes >The structure, function and regulation of the nodulin 26-like intrinsic protein family of plant aquaglyceroporins
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The structure, function and regulation of the nodulin 26-like intrinsic protein family of plant aquaglyceroporins

机译:植物水甘油糖蛋白Nodulin 26样内在蛋白家族的结构,功能和调控

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The nodulin 26-like intrinsic protein family is a group of highly conserved multifunctional major intrinsic proteins that are unique to plants, and which transport a variety of uncharged solutes ranging from water to ammonia to glycerol. Based on structure-function studies, the NIP family can be subdivided into two subgroups (I and II) based on the identity of the amino acids in the selectivity-determining filter (ar/R region) of the transport pore. Both subgroups appear to contain multifunctional transporters with low to no water permeability and the ability to flux multiple uncharged solutes of varying sizes depending upon the composition of the residues of the ar/R filter. NIPs are subject to posttranslational phosphorylation by calcium-dependent protein kinases. In the case of the family archetype, soybean nodulin 26, phosphorylation has been shown to stimulate its transport activity and to be regulated in response to developmental as well as environmental cues, including osmotic stresses. NIPs tend to be expressed at low levels in the plant compared to other MIPs, and several exhibit cell or tissue specific expression that is subject to spatial and temporal regulation during development. (c) 2006 Elsevier B.V. All rights reserved.
机译:结节蛋白26样内在蛋白质家族是一组高度保守的多功能主要内在蛋白质,对植物而言是独特的,并且运输从水到氨再到甘油的各种不带电荷的溶质。根据结构功能研究,可以根据转运孔的选择性决定性过滤器(ar / R区域)中氨基酸的身份将NIP家族分为两个亚组(I和II)。两个亚组似乎都包含多功能转运蛋白,其渗透性低至无,并且能够根据ar / R过滤器残渣的组成使大小不等的多种不带电荷的溶质通量。 NIP受钙依赖性蛋白激酶的翻译后磷酸化作用。就家庭原型大豆结节蛋白26而言,磷酸化已显示出可刺激其运输活性,并受发育和环境因素(包括渗透压)的影响而受到调节。与其他MIP相比,NIP倾向于在植物中以低水平表达,并且某些NIP表现出细胞或组织特异性表达,而这些表达在发育过程中受到时空调节。 (c)2006 Elsevier B.V.保留所有权利。

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