Nucleocytoplasmic transport of proteins

Biochemistry (Mosc). 2007 Dec;72(13):1439-57. doi: 10.1134/s0006297907130032.

Abstract

In eukaryotic cells, the movement of macromolecules between the nucleus and cytoplasm occurs through the nuclear pore complex (NPC)--a large protein complex spanning the nuclear envelope. The nuclear transport of proteins is usually mediated by a family of transport receptors known as karyopherins. Karyopherins bind to their cargoes via recognition of nuclear localization signal (NLS) for nuclear import or nuclear export signal (NES) for export to form a transport complex. Its transport through NPC is facilitated by transient interactions between the karyopherins and NPC components. The interactions of karyopherins with their cargoes are regulated by GTPase Ran. In the current review, we describe the NPC structure, NLS, and NES, as well as the model of classic Ran-dependent transport, with special emphasis on existing alternative mechanisms; we also propose a classification of the basic mechanisms of protein transport regulation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Active Transport, Cell Nucleus*
  • Animals
  • Arabidopsis / genetics
  • Cytoplasm / metabolism
  • Drosophila melanogaster
  • Humans
  • Karyopherins / metabolism
  • Models, Biological
  • Nuclear Localization Signals
  • Nuclear Pore*
  • Protein Binding
  • RNA Interference
  • Transgenes
  • ran GTP-Binding Protein / metabolism

Substances

  • Karyopherins
  • Nuclear Localization Signals
  • ran GTP-Binding Protein