Nuclear pore structure and function.
Nuclear pores are huge macromolecular assemblies, approximately 120 nm in diameter, that perforate the nuclear membrane and mediate nucleocytoplasmic transport. Nuclear pores are constructed from a cylindrical spoke-plug complex sandwiched between nucleoplasmic and cytoplasmic rings. The spoke-plug complex has pronounced 8-fold rotational symmetry, which is also present in the rings. Nucleocytoplasmic transport is an energy-requiring process that takes place through the centre of the pores and can accommodate particles up to about 25 nm diameter. Translocation is preceded by a separate binding step which does not require energy. Several nuclear pore proteins have been isolated and characterized. Many of these proteins contain O-linked N-acetyl glucosamine residues and may have similar modular domain structures.
Stewart
M
M
MRC Laboratory of Molecular Biology, Cambridge, UK.
D000818:Animals; D001692:Biological Transport; D002467:Cell Nucleus / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000502:physiology; D008854:Microscopy, Electron / Q000379:methods; D008970:Molecular Weight; D009685:Nuclear Envelope / Q000502:physiology* / Q000648:ultrastructure*; D009687:Nuclear Proteins / Q000502:physiology
D008562:Membrane Glycoproteins; D009687:Nuclear Proteins