Interaction between a plasma membrane-localized ankyrin-repeat protein ITN1 and a nuclear protein RTV1

Interaction between a plasma membrane-localized ankyrin-repeat protein ITN1 and a nuclear protein RTV1
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质膜定位锚蛋白重复蛋白 ITN1 和核蛋白 RTV1 之间的相互作用

DOI:
10.1016/j.bbrc.2012.05.136
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发表时间:
2012
期刊:
Biochemistry Biophysics Research CommunicationBiochemistry Biophysics Research Communication
影响因子:
--
通讯作者:
K.
K.
中科院分区:
--
文献类型:
--
作者:
Sakamoto;H.;Sakata;K.;Kusumi;K.;Kojima;M.;Sakakibara;H. and Iba;K.

文献摘要

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耐盐性增强蛋白(ITN1)是一种定位于细胞膜的蛋白,参与了拟南芥对盐胁迫的响应。ITN1的预测结构由多个跨膜区和一个已知介导蛋白质-蛋白质相互作用的Ankyrin-Repeat结构域组成。为了阐明ITN1的分子功能,我们利用酵母双杂交技术寻找相互作用的伙伴,并确定了一个核定位的DNA结合蛋白RTV1。双分子荧光互补分析表明,RTV1在活体内与ITN1在质膜和胞核相互作用。红色荧光蛋白标记的RTV1定位于细胞核,ITN1标记的绿色荧光蛋白定位于PM;然而,当两者共同表达时,这两种蛋白都定位于细胞核和PM。这些发现表明RTV1和ITN1相互调节彼此的亚细胞定位。
The increased tolerance to NaCl 1 (ITN1) protein is a plasma membrane (PM)-localized protein involved in responses to NaCl stress in Arabidopsis. The predicted structure of ITN1 is composed of multiple transmembrane regions and an ankyrin-repeat domain that is known to mediate protein–protein interactions. To elucidate the molecular functions of ITN1, we searched for interacting partners using a yeast two-hybrid assay, and a nuclear-localized DNA-binding protein, RTV1, was identified as a candidate. Bimolecular fluorescence complementation analysis revealed that RTV1 interacted with ITN1 at the PM and nuclei in vivo. RTV1 tagged with red fluorescent protein localized to nuclei and ITN1 tagged with green fluorescent protein localized to PM; however, both proteins localized to both nuclei and the PM when co-expressed. These findings suggest that RTV1 and ITN1 regulate the subcellular localization of each other.