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A gtpase distinct from ran is involved in nuclear protein import

Academic Article
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Overview

authors

  • Sweet, D. J.
  • Gerace, Larry

publication date

  • June 1996

journal

  • Journal of Cell Biology  Journal

abstract

  • Signal-dependent transport of proteins into the nucleus is a multi-step process mediated by nuclear pore complexes and cytosolic transport factors. One of the cytosolic factors, Ran, is the only GTPase that has a characterized role in the nuclear import pathway. We have used a mutant form of Ran with altered nucleotide binding specificity to investigate whether any other GTPases are involved in nuclear protein import. D125N Ran (XTP-Ran) binds specifically to xanthosine triphosphate (XTP) and has a greatly reduced affinity for GTP, so it is no longer sensitive to inhibition by nonhydrolyzable analogues of GTP such as guanosine 5'-O-(3-thiotriphosphate) (GTP gamma S). using in vitro transport assays, we have found that nuclear import supported by XTP-Ran is nevertheless inhibited by the addition of non-hydrolyzable GTP analogues. This in conjunction with the properties of the inhibitory effect indicates that at least one additional GTPase is involved in the import process. Initial characterization suggests that the inhibited GTPase plays a direct role in protein import and could be a component of the nuclear pore complex.

subject areas

  • Biological Transport, Active
  • Cytosol
  • GTP Phosphohydrolases
  • Guanosine Triphosphate
  • HeLa Cells
  • Humans
  • Nuclear Envelope
  • Nuclear Proteins
  • Nucleotides
  • Point Mutation
  • Ribonucleotides
  • ran GTP-Binding Protein
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Identity

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.133.5.971

PubMed ID

  • 8655588
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Additional Document Info

start page

  • 971

end page

  • 983

volume

  • 133

issue

  • 5

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