The dynamics of karyopherin-mediated nuclear transport

Biochem Cell Biol. 2001;79(5):603-12.


The regulated exchange of proteins and nucleic acids between the nucleus and cytoplasm demands a complex interplay between nuclear pore complexes (NPCs), which provide conduits in the nuclear envelope, and mobile transport receptors (or karyopherins, also known as importins/exportins) that bind and mediate the translocation of cargoes through the NPCs. Biochemical characterization of individual karyopherins has led to the identification of many of their cargoes and to the elucidation of the mechanisms by which they mediate transport. Likewise, the characterization of numerous NPC-associated components, in combination with structural studies of NPCs, have begun to address the possible mechanisms that drive nucleocytoplasmic transport, and the role that different nucleoporins play in the transport process. Some recent studies indicate that several NPC-associated factors, previously thought to be stable components of the NPC, dynamically interact with both nuclear and cytoplasmic aspects of the NPC. The mobility of these components challenges our conventional view of the NPC as the stationary phase of transport. These components and their potiential roles in nucleo-cytoplasmic transport are discussed.

Publication types

  • Review

MeSH terms

  • Active Transport, Cell Nucleus*
  • Animals
  • Cytoplasm / metabolism
  • Models, Biological
  • Nuclear Envelope / metabolism*
  • Nuclear Pore Complex Proteins / metabolism
  • Protein Transport
  • Saccharomyces cerevisiae Proteins / metabolism
  • beta Karyopherins / metabolism*


  • NUP2 protein, S cerevisiae
  • Nuclear Pore Complex Proteins
  • Saccharomyces cerevisiae Proteins
  • beta Karyopherins