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lüll Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import Stewart M; Baker RP; Bayliss R; Clayton L; Grant RP; Littlewood T; Matsuura YFEBS Lett 2001[Jun]; 498 (2-3): 145-9The 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.|Active Transport, Cell Nucleus/*physiology[MESH]|Animals[MESH]|Cell Nucleus/physiology[MESH]|Karyopherins[MESH]|Models, Biological[MESH]|Nuclear Pore/*metabolism[MESH]|Nuclear Proteins/*metabolism[MESH]|ran GTP-Binding Protein/metabolism[MESH] |