Molecular dissection of the nuclear pore complex.
The nuclear pore complex (NPC) is an approximately 120 megadalton (MDa) supramolecular assembly embedded in the double-membraned nuclear envelope (NE) that mediates bidirectional molecular trafficking between the cytoplasm and the nucleus of interphase eukaryotic cells. The structure of the NPC has been studied extensively by electron microscopy (EM), and a consensus model of its basic framework has emerged. Over the past few years, there has been significant progress in dissecting the molecular constituents of the NPC and in identifying distinct NPC subcomplexes. The combination of well-characterized antibodies with different EM specimen preparation methods has allowed localization of several of these proteins within the three-dimensional (3-D) architecture of the NPC. Thus, the molecular dissection of the NPC is definitely on its way to being elucidated. Here, we review these findings and discuss the emerging structural concepts.
Panté
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M.E. Müller Institute for Microscopy, Biozentrum, University of Basel, Switzerland.
Aebi
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D000595:Amino Acid Sequence; D000818:Animals; D001692:Biological Transport; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*; D008969:Molecular Sequence Data; D009685:Nuclear Envelope / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*; D009687:Nuclear Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*
D008565:Membrane Proteins; D009687:Nuclear Proteins