Interaction between importin 13 and myopodin suggests a nuclear import pathway for myopodin
Interaction between importin 13 and myopodin suggests a nuclear import pathway for myopodin
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输入蛋白 13 和肌足蛋白之间的相互作用表明肌足蛋白的核输入途径
DOI：
10.1007/s11010-007-9588-1
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发表时间：
2008-01-01
影响因子：
4.3
通讯作者：
Tao, Tao
中科院分区：
文献类型：
--
作者：
Liang, Jie;Ke, Guifen;Tao, Tao
Importin 13是核转运蛋白importin β超家族的成员，在人类和啮齿类动物的多种组织中以高水平表达，包括胎儿肺、脑和心脏。为了阐明imp 13在心脏中的潜在功能，我们使用大鼠imp 13作为诱饵筛选人心脏cDNA文库，并鉴定了与肌足蛋白C-末端肽（a.a. 360-698），一种肌动蛋白捆绑蛋白，与定位于细胞质和细胞核的肿瘤抑制活性相关。我们已经使用GST-下拉测定和免疫共沉淀实验来证明imp 13和全长肌足蛋白之间的相互作用，并观察到RanGTP解离的肌足蛋白imp 13复合物。在培养细胞的研究中，我们发现，imp 13 siRNA和imp 13蛋白的C-末端片段阻止肌足蛋白的核定位。因此，我们得出结论，IMP 13功能的肌足蛋白进口，我们认为，这些事件的调节是至关重要的正常和异常的细胞分化。
Importin 13 is a member of the importin β superfamily of nuclear transport proteins and is expressed in multiple tissues at high levels both in humans and rodents, including fetal lung, brain, and heart. In order to elucidate potential functions of imp13 in the heart, we have used rat imp13 as bait to screen a human heart cDNA library and identified an interaction with the C-terminal peptide of myopodin (a.a. 360–698), an actin-bundling protein, associated with tumor–suppressor activity that localizes to both the cytoplasm and the nucleus. We have used GST-pull down assays and co-immunoprecipitation experiments to demonstrate an interaction between imp13 and full-length myopodin and observed that RanGTP dissociates the myopodin–imp13 complex. In studies of cultured cells, we show that both imp13 siRNA and a C-terminal fragment of imp13 protein prevent nuclear localization of myopodin. We, therefore, conclude that imp13 functions in myopodin import and we suggest that the regulation of these events is critical for normal and abnormal cellular differentiation.