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Published online 28 July 2003. doi:10.1083/jcb.200303085
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© The Rockefeller University Press, 0021-9525/2003/8/391 $5.00
The Journal of Cell Biology, Volume 162, Number 3, 391-401

Article

Importin ß contains a COOH-terminal nucleoporin binding region important for nuclear transport



Janna Bednenko, Gino Cingolani and Larry Gerace

Department of Cell Biology and Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037

Address correspondence to Larry Gerace, The Scripps Research Institute, IMM-10, 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: (858) 784-8514. Fax: (858) 784-9132. email: lgerace{at}scripps.edu

Proteins containing a classical NLS are transported into the nucleus by the import receptor importin ß, which binds to cargoes via the adaptor importin {alpha}. The import complex is translocated through the nuclear pore complex by interactions of importin ß with a series of nucleoporins. Previous studies have defined a nucleoporin binding region in the NH2-terminal half of importin ß. Here we report the identification of a second nucleoporin binding region in its COOH-terminal half. Although the affinity of the COOH-terminal region for nucleoporins is dramatically weaker than that of the NH2-terminal region, sets of mutations that perturb the nucleoporin binding of either region reduce the nuclear import activity of importin ß to a similar extent (~50%). An importin ß mutant with a combination of mutations in the NH2- and COOH-terminal regions is completely inactive for nuclear import. Thus, importin ß possesses two nucleoporin binding sites, both of which are important for its nuclear import function.

Key Words: nuclear import; importin ß; nucleoporin; Ran; site-directed mutagenesis

The online version of this article includes supplemental material.

Abbreviations used in this paper: IBB, importin ß binding; NPC, nuclear pore complex; PTHrP, parathyroid hormone–related protein.


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