title: Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import.
abstract: The trafficking of macromolecules between cytoplasm and nucleus through nuclear pore complexes is mediated by specific carrier molecules such as members of the importin-beta family. Nuclear pore proteins (nucleoporins) frequently contain sequence repeats based on FG cores and carriers appear to move their cargo through the pores by hopping between successive FG cores. A major question is why some macromolecules are transported while others are not. This selectivity may be generated by the ability to bind FG repeats, a local concentration of carrier-cargo complexes near the entrance to the pore channel, and steric hindrance produced by high concentrations of nucleoporins in the channel.
authors: MRC Laboratory of Molecular Biology, Hills Rd., CB2 2QH, Cambridge, UK. ms@mrc-lmb.cam.ac.uk
authors: M
authors: M
authors: Stewart
authors: R P
authors: RP
authors: Baker
authors: R
authors: R
authors: Bayliss
authors: L
authors: L
authors: Clayton
authors: R P
authors: RP
authors: Grant
authors: T
authors: T
authors: Littlewood
authors: Y
authors: Y
authors: Matsuura
mesh_terms: D021581:Active Transport, Cell Nucleus / Q000502:physiology*; D000818:Animals; D002467:Cell Nucleus / Q000502:physiology; D028884:Karyopherins; D008954:Models, Biological; D022022:Nuclear Pore / Q000378:metabolism*; D009687:Nuclear Proteins / Q000378:metabolism*; D020931:ran GTP-Binding Protein / Q000378:metabolism
chemical_list: D028884:Karyopherins; D009687:Nuclear Proteins; D020931:ran GTP-Binding Protein