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Influence of cargo size on ran and energy requirements for nuclear protein import

Academic Article
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Overview

authors

  • Lyman, S. K.
  • Guan, T. L.
  • Bednenko, J.
  • Wodrich, H.
  • Gerace, Larry

publication date

  • October 2002

journal

  • Journal of Cell Biology  Journal

abstract

  • Previous work has shown that the transport of some small protein cargoes through the nuclear pore complex (NPC) can occur in vitro in the absence of nucleoside triphosphate hydrolysis. We now demonstrate that in the importin alpha/beta and transportin import pathways, efficient in vitro transport of large proteins, in contrast to smaller proteins, requires hydrolyzable GTP and the small GTPase Ran. Morphological and biochemical analysis indicates that the presence of Ran and GTP allows large cargo to efficiently cross central regions of the NPC. We further demonstrate that this function of RanGTP at least partly involves its direct binding to importin beta and transportin. We suggest that RanGTP functions in these pathways to promote the transport of large cargo by enhancing the ability of import complexes to traverse diffusionally restricted areas of the NPC.

subject areas

  • Active Transport, Cell Nucleus
  • Binding Sites
  • Cell Nucleus
  • Guanosine Triphosphate
  • HeLa Cells
  • Humans
  • Molecular Weight
  • Nuclear Pore
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins
  • alpha Karyopherins
  • beta Karyopherins
  • ran GTP-Binding Protein
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Research

keywords

  • Ran
  • importin beta
  • nuclear protein import
  • nucleoporin
  • transportin
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Identity

PubMed Central ID

  • PMC2173498

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.200204163

PubMed ID

  • 12370244
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Additional Document Info

start page

  • 55

end page

  • 67

volume

  • 159

issue

  • 1

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