Involvement of human CRM1 (exportin 1) in the export and multimerization of the Rex protein of human T-cell leukemia virus type 1
Involvement of human CRM1 (exportin 1) in the export and multimerization of the Rex protein of human T-cell leukemia virus type 1
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DOI：
10.1128/jvi.72.8.6602-6607.1998
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发表时间：
1998-08-01
影响因子：
5.4
通讯作者：
Shida, H
中科院分区：
文献类型：
--
作者：
Hakata, Y;Umemoto, T;Shida, H
我们研究了人CRM1（hCRM1）（exportin 1）在人T细胞白血病病毒1型编码的雷克斯蛋白功能中的作用。hCRM 1促进了雷克斯蛋白从细胞核向细胞质的输出。在活化结构域中具有突变的雷克斯蛋白RexM90丧失了与hCRM 1结合的能力和多聚化的能力。hCRM 1的过表达补充了RexM 64的功能缺陷，RexM 64在雷克斯的多聚化结构域中含有突变。一个显性负性的雷克斯的突变体，螯合辅因子的雷克斯废除多聚化以及活性的野生型雷克斯蛋白。这两个功能同时恢复hCRM 1的过表达。综上所述，这些结果表明hCRM 1在雷克斯蛋白的多聚化和输出中起重要作用。
We investigated the role of human CRM1 (hCRM1) (exportin 1) in the function of Rex protein encoded by human T-cell leukemia virus type 1. hCRM1 promoted the export of Rex protein from the nucleus to the cytoplasm. A Rex protein with a mutation in the activation domain, RexM90, lost both the ability to hind to hCRM1 and the ability to multimerize. The overexpression of hCRM1 complemented the functional defects of RexM64, which contains a mutation in the multimerization domain of Rex. A dominant-negative mutant of Rex which sequesters cofactors of Rex abrogated multimerization as well as the activity of the wild-type Rex protein. These two functions were simultaneously restored by the overexpression of hCRM1. Taken together, these results suggest that hCRM1 plays important roles in the multimerization and export of Rex protein.