title: Exploring nuclear pore complex structure and function in molecular detail.
abstract: Bidirectional molecular trafficking between the nucleus and the cytoplasm of eukaryotic cells occurs through the nuclear pore complexes (NPCs), approximately 120 megadalton supramolecular assemblies embedded in the double-membraned nuclear envelope. Significant progress has been made in elucidating the three-dimensional (3-D) architecture of the NPC, and in identifying, characterizing, and cloning and sequencing NPC proteins. Several of these have now been localized within the 3-D structure of the NPC. Nevertheless, there still remain major questions relating to the conformation, molecular composition and functional roles of distinct NPC components. Here we review recent structural studies from our group and others which have contributed toward dissecting the molecular architecture of the NPC. We also present our results on the molecular characterization of some NPC components, and on the elucidation of their functional roles in mediated nucleocytoplasmic transport.
authors.affiliation: M. E. Müller Institute for Microscopy, Biozentrum, University of Basel, Switzerland.
authors.forename: N
authors.initials: N
authors.lastname: Panté
authors.forename: U
authors.initials: U
authors.lastname: Aebi
mesh_terms: D000818:Animals; D001692:Biological Transport; D046911:Macromolecular Substances; D009685:Nuclear Envelope / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*; D009687:Nuclear Proteins / Q000737:chemistry* / Q000502:physiology*; D014981:Xenopus
chemical_list: D046911:Macromolecular Substances; D009687:Nuclear Proteins