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Phosphorylation of the nuclear transport machinery down-regulates nuclear protein import in vitro

Academic Article
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Overview

authors

  • Kehlenbach, R. H.
  • Gerace, Larry

publication date

  • June 2000

journal

  • Journal of Biological Chemistry  Journal

abstract

  • We have examined whether signal-mediated nucleocytoplasmic transport can be regulated by phosphorylation of the nuclear transport machinery. Using digitonin-permeabilized cell assays to measure nuclear import and export, we found that the phosphatase inhibitors okadaic acid and microcystin inhibit transport mediated by the import receptors importin beta and transportin, but not by the export receptor CRM1. Several lines of evidence, including the finding that transport inhibition is partially reversed by the broad specificity protein kinase inhibitor staurosporine, indicate that transport inhibition is due to elevated phosphorylation of a component of the nuclear transport machinery. The kinases and phosphatases involved in this regulation are present in the permeabilized cells. A phosphorylation-sensitive component of the nuclear transport machinery also is present in permeabilized cells and is most likely a component of the nuclear pore complex. Substrate binding by the importin alpha.beta complex and the association of the complex with the nucleoporins Nup358/RanBP2 and Nup153 are not affected by phosphatase inhibitors, suggesting that transport inhibition by protein phosphorylation does not involve these steps. These results suggest that cells have mechanisms to negatively regulate entire nuclear transport pathways, thus providing a means to globally control cellular activity through effects on nucleocytoplasmic trafficking.

subject areas

  • Adenosine Triphosphate
  • Carrier Proteins
  • Cell Membrane Permeability
  • Cell Nucleus
  • Enzyme Inhibitors
  • HeLa Cells
  • Humans
  • Karyopherins
  • Kinetics
  • Microcystins
  • Nuclear Envelope
  • Nuclear Proteins
  • Okadaic Acid
  • Peptides, Cyclic
  • Phosphorylation
  • Protein Kinases
  • Receptors, Cytoplasmic and Nuclear
  • Thionucleotides
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M001455200

PubMed ID

  • 10749866
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Additional Document Info

start page

  • 17848

end page

  • 17856

volume

  • 275

issue

  • 23

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