Cloning and characterization of human karyopherin beta3.
Nuclear import of classical nuclear localization sequence-bearing proteins is mediated by karyopherin alpha/beta1 heterodimers. A second nuclear import pathway, mediated by karyopherin beta2 (transportin), recently was described for mRNA-binding proteins. Here we report the cloning and characterization of human karyopherin beta3, which may be involved in a third pathway for nuclear import. Karyopherin beta3 was localized mainly to the cytosol and the nucleus, particularly the nuclear rim. It bound to several of the repeat-containing nucleoporins (Nup358, Nup214, Nup153, Nup98, and p62) in overlay and solution-binding assays and was competed away by karyopherin beta1. For Nup98, we localized this binding to the peptide repeat-containing region. Karyopherin beta3 contains two putative Ran-binding homology regions and bound to Ran-GTP in a solution-binding assay with much higher affinity than to Ran-GDP. Furthermore, it interacted with two ribosomal proteins in an overlay assay. We suggest that karyopherin beta3 is a nuclear transport factor that may mediate the import of some ribosomal proteins into the nucleus.[1]References
- Cloning and characterization of human karyopherin beta3. Yaseen, N.R., Blobel, G. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
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