小扁豆种子水通道蛋白形成一种异源寡聚体，该异源寡聚体被一种Mg(2+)依赖且Ca(2+)调节的激酶磷酸化。
Lentil seed aquaporins form a hetero-oligomer which is phosphorylated by a Mg(2+)-dependent and Ca(2+)-regulated kinase.
作者信息
Harvengt P, Vlerick A, Fuks B, Wattiez R, Ruysschaert J M, Homble F
机构信息
Laboratoire de Physiologie Végétale, CP 206/2, Faculté des Sciences, Université Libre de Bruxelles, Bld du Triomphe, B-1050 Brussels, Belgium.
出版信息
Biochem J. 2000 Nov 15;352 Pt 1(Pt 1):183-90.
Abstract
In plants, aquaporins regulate the water flow through membranes during growth, development and stress responses. We have isolated two isoforms of the aquaporin family from the protein-storage vacuoles of lentil (Lens culinaris Med.) seeds. Chemical cross-linking experiments showed that both isoforms belong to the same oligomer in the membrane and are phosphorylated by a membrane-bound protein kinase. We assigned the kinase activity to a 52 kDa protein that is magnesium-dependent and calcium-regulated.
摘要
在植物中，水通道蛋白在生长、发育和应激反应过程中调节水分通过膜的流动。我们从扁豆（Lens culinaris Med.）种子的蛋白储存液泡中分离出了水通道蛋白家族的两种亚型。化学交联实验表明，这两种亚型在膜中属于同一寡聚体，并被一种膜结合蛋白激酶磷酸化。我们将该激酶活性归因于一种52 kDa的蛋白，该蛋白依赖镁且受钙调节。
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An abundant, highly conserved tonoplast protein in seeds.种子中一种丰富且高度保守的液泡膜蛋白。
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Projection structure of a plant vacuole membrane aquaporin by electron cryo-crystallography.利用电子冷冻晶体学解析植物液泡膜水通道蛋白的投影结构
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