title: The mechanism of nucleocytoplasmic transport through the nuclear pore complex.
abstract: The nuclear pore complex (NPC) mediates all transport between the nucleus and cytoplasm. Passage through the NPC is highly selective, yet the same channel must allow rapid specific transport of a wide range of cargoes. This chapter focuses mainly on the phenylalanine-glycine (FG) nucleoporins (nups), proteins carrying natively unfolded regions that are thought to form the selectively permeable barrier within the NPC. The physical properties of the FG nup barrier remain unclear. The high selectivity and rapidity of transport observed in vivo may be explained, in part, by competition for binding and space between transport factors and nontransported proteins. Future studies of FG nups will therefore also examine their interactions between FG nups and other proteins in their surroundings.
authors: Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, New York 10065, USA.
authors: J
authors: J
authors: Tetenbaum-Novatt
authors: M P
authors: MP
authors: Rout
mesh_terms: D021581:Active Transport, Cell Nucleus; D000818:Animals; D001665:Binding Sites; D005998:Glycine / Q000378:metabolism; D006801:Humans; D008954:Models, Biological; D022022:Nuclear Pore / Q000737:chemistry / Q000378:metabolism*; D028861:Nuclear Pore Complex Proteins / Q000737:chemistry / Q000378:metabolism; D010649:Phenylalanine / Q000378:metabolism; D011485:Protein Binding; D020449:Repetitive Sequences, Amino Acid; D012995:Solubility
chemical_list: D028861:Nuclear Pore Complex Proteins; D010649:Phenylalanine; D005998:Glycine