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Importin beta contains a cooh-terminal nucleoporin binding region important for nuclear transport

Academic Article
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Overview

authors

  • Bednenko, J.
  • Cingolani, G.
  • Gerace, Larry

publication date

  • August 2003

journal

  • Journal of Cell Biology  Journal

abstract

  • Proteins containing a classical NLS are transported into the nucleus by the import receptor importin beta, which binds to cargoes via the adaptor importin alpha. The import complex is translocated through the nuclear pore complex by interactions of importin beta with a series of nucleoporins. Previous studies have defined a nucleoporin binding region in the NH2-terminal half of importin beta. 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 beta to a similar extent ( approximately 50%). An importin beta mutant with a combination of mutations in the NH2- and COOH-terminal regions is completely inactive for nuclear import. Thus, importin beta possesses two nucleoporin binding sites, both of which are important for its nuclear import function.

subject areas

  • Active Transport, Cell Nucleus
  • Amino Acids
  • Binding Sites
  • Carboxylic Acids
  • Down-Regulation
  • Eukaryotic Cells
  • HeLa Cells
  • Humans
  • Nuclear Pore
  • Nuclear Pore Complex Proteins
  • Point Mutation
  • Protein Structure, Tertiary
  • Protein Transport
  • beta Karyopherins
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Research

keywords

  • Ran
  • importin beta
  • nuclear import
  • nucleoporin
  • site-directed mutagenesis
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Identity

PubMed Central ID

  • PMC2172684

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.200303085

PubMed ID

  • 12885761
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Additional Document Info

start page

  • 391

end page

  • 401

volume

  • 162

issue

  • 3

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