PMID: 9658105Jul 11, 1998Paper

Involvement of human CRM1 (exportin 1) in the export and multimerization of the Rex protein of human T-cell leukemia virus type 1

Journal of Virology
Yoshiyuki HakataHisatoshi Shida

Abstract

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.

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Citations

Apr 14, 2004·Journal of Virology·Rozanne M Sandri-Goldin
Sep 13, 2005·Oncogene·Fatah Kashanchi, John N Brady
Mar 16, 2007·The Journal of Biological Chemistry·Uma Sinha-DattaChristophe Nicot
Jan 22, 2011·Genes to Cells : Devoted to Molecular & Cellular Mechanisms·Mika Nagai-FukatakiHisatoshi Shida
Dec 6, 2012·Leukemia Research and Treatment·Francesca RendeVincenzo Ciminale
Mar 2, 2016·Viruses·Kazumi Nakano, Toshiki Watanabe
Apr 29, 2009·Reviews in Medical Virology·Anna Greco
Apr 25, 2020·Pathogens·Léa ProchassonVincent Mocquet
Nov 12, 2003·Journal of Virology·Murli NarayanPatrick L Green
Apr 5, 2001·FEBS Letters·A BoeseN Mueller-Lantzsch
Nov 19, 2009·Retrovirology·Matthew KesicPatrick L Green
Nov 10, 1998·Genes & Development·F Stutz, M Rosbash

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