JCB logo
16th INTERNATIONAL VASCULAR BIOLOGY MEETING
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online 28 July 2003. doi:10.1083/jcb.200303085
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 312K)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bednenko, J.
Right arrow Articles by Gerace, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bednenko, J.
Right arrow Articles by Gerace, L.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

© 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.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents