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J Virol, August 1998, p. 6602-6607, Vol. 72, No. 8
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Involvement of Human CRM1 (Exportin 1) in the Export and Multimerization of the Rex Protein of Human T-Cell Leukemia Virus Type 1

Yoshiyuki Hakata,1 Tomoe Umemoto,1 Shuzo Matsushita,2 and Hisatoshi Shida1,*

Institute for Virus Research, Kyoto University, Kyoto 606,1 and The Second Department of Internal Medicine, Kumamoto University Medical School, Kumamoto 860,2 Japan

Received 3 March 1998/Accepted 5 May 1998

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 bind 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.

* Corresponding author. Mailing address: Institute for Virus Research, Kyoto University, Kyoto 606, Japan. Phone: 81-75-751-4016. Fax: 81-75-761-5626. E-mail: hshida{at}virus.kyoto-u.ac.jp.

J Virol, August 1998, p. 6602-6607, Vol. 72, No. 8
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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