Structural basis for assembly and disassembly of the CRM1 nuclear export complex

Nat Struct Mol Biol. 2009 May;16(5):558-60. doi: 10.1038/nsmb.1586. Epub 2009 Apr 1.

Abstract

CRM1 (or exportin 1, Xpo1) transports proteins out of the cell nucleus through the nuclear pore complex. In the cytoplasm, GTP hydrolysis and consequent dissociation of Ran from CRM1 releases low-affinity substrates, while additional factors facilitate release of high-affinity substrates. Here we provide a model for human CRM1 export complex assembly and disassembly through structural and biochemical analyses of CRM1 bound to the substrate snurportin 1 (SNUPN, also called snuportin 1).

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Active Transport, Cell Nucleus
  • Cell Nucleus / metabolism*
  • Humans
  • Karyopherins / chemistry*
  • Karyopherins / metabolism*
  • Ligands
  • Models, Molecular
  • Protein Binding
  • Protein Structure, Secondary
  • RNA Cap-Binding Proteins / metabolism
  • RNA Caps / metabolism
  • Receptors, Cytoplasmic and Nuclear / chemistry*
  • Receptors, Cytoplasmic and Nuclear / metabolism*
  • Substrate Specificity
  • ran GTP-Binding Protein / metabolism

Substances

  • Karyopherins
  • Ligands
  • RNA Cap-Binding Proteins
  • RNA Caps
  • Receptors, Cytoplasmic and Nuclear
  • SNUPN protein, human
  • exportin 1 protein
  • ran GTP-Binding Protein