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Published online 3 January 2002. doi:10.1083/jcb.200110082
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© The Rockefeller University Press, 0021-9525/2002/1/53 $5.00
The Journal of Cell Biology, Volume 156, Number 1, January 7, 2002 53-64

Article

Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins



Amy M. Brownawell and Ian G. Macara

Center for Cell Signaling, University of Virginia, Charlottesville, VA 22908

Address correspondence to Amy M. Brownawell, University of Virginia, Center for Cell Signaling, Hospital West Rm. 7191, P.O. Box 800577 HSC, Charlottesville, VA 22908. Tel.: (434) 982-0083. Fax: (434) 924-1236. E-mail: amb7c{at}virginia.edu

We have identified a novel human karyopherin (Kap)ß family member that is related to human Crm1 and the Saccharomyces cerevisiae protein, Msn5p/Kap142p. Like other known transport receptors, this Kap binds specifically to RanGTP, interacts with nucleoporins, and shuttles between the nuclear and cytoplasmic compartments. We report that interleukin enhancer binding factor (ILF)3, a double-stranded RNA binding protein, associates with this Kap in a RanGTP-dependent manner and that its double-stranded RNA binding domain (dsRBD) is the limiting sequence required for this interaction. Importantly, the Kap interacts with dsRBDs found in several other proteins and binding is blocked by double-stranded RNA. We find that the dsRBD of ILF3 functions as a novel nuclear export sequence (NES) in intact cells, and its ability to serve as an NES is dependent on the expression of the Kap. In digitonin-permeabilized cells, the Kap but not Crm1 stimulated nuclear export of ILF3. Based on the ability of this Kap to mediate the export of dsRNA binding proteins, we named the protein exportin-5. We propose that exportin-5 is not an RNA export factor but instead participates in the regulated translocation of dsRBD proteins to the cytoplasm where they interact with target mRNAs.

Key Words: exportin-5; nuclear export; ILF3; double-stranded RNA binding domains; mRNA localization


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