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      The Yeast Nuclear Pore Complex : Composition, Architecture, and Transport Mechanism

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          Abstract

          An understanding of how the nuclear pore complex (NPC) mediates nucleocytoplasmic exchange requires a comprehensive inventory of the molecular components of the NPC and a knowledge of how each component contributes to the overall structure of this large molecular translocation machine. Therefore, we have taken a comprehensive approach to classify all components of the yeast NPC (nucleoporins). This involved identifying all the proteins present in a highly enriched NPC fraction, determining which of these proteins were nucleoporins, and localizing each nucleoporin within the NPC. Using these data, we present a map of the molecular architecture of the yeast NPC and provide evidence for a Brownian affinity gating mechanism for nucleocytoplasmic transport.

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          Most cited references72

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          Forced thermal ratchets.

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            Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum

            A rapid and simple method for the isolation of membranes from subcellular organelles is described. The procedure consists of diluting the organelles in ice-cold 100 mM Na2CO3 followed by centrifugation to pellet the membranes. Closed vesicles are converted to open membrane sheets, and content proteins and peripheral membrane proteins are released in soluble form. Here we document the method by applying it to various subfractions of a rat liver microsomal fraction, prepared by continuous density gradient centrifugation according to Beaufay et al. (1974, J. Cell Biol. 61:213-231). The results confirm and extend those of previous investigators on the distribution of enzymes and proteins among the membranes of the smooth and rough endoplasmic reticulum. In the accompanying paper (1982, J. Cell Biol. 93:103-110) the procedure is applied to peroxisomes and mitochondria.
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              Nucleocytoplasmic transport: the soluble phase.

              Active transport between the nucleus and cytoplasm involves primarily three classes of macromolecules: substrates, adaptors, and receptors. Some transport substrates bind directly to an import or an export receptor while others require one or more adaptors to mediate formation of a receptor-substrate complex. Once assembled, these transport complexes are transferred in one direction across the nuclear envelope through aqueous channels that are part of the nuclear pore complexes (NPCs). Dissociation of the transport complex must then take place, and both adaptors and receptors must be recycled through the NPC to allow another round of transport to occur. Directionality of either import or export therefore depends on association between a substrate and its receptor on one side of the nuclear envelope and dissociation on the other. The Ran GTPase is critical in generating this asymmetry. Regulation of nucleocytoplasmic transport generally involves specific inhibition of the formation of a transport complex; however, more global forms of regulation also occur.
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                Author and article information

                Contributors
                Journal
                J Cell Biol
                The Journal of Cell Biology
                The Rockefeller University Press
                0021-9525
                1540-8140
                21 February 2000
                : 148
                : 4
                : 635-652
                Affiliations
                [a ]The Rockefeller University, New York, NY 10021
                [b ]Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada
                Article
                1075
                10.1083/jcb.148.4.635
                2169373
                10684247
                805ecc95-5433-4c73-8544-d8760ff5eb80
                © 2000 The Rockefeller University Press
                History
                : 18 January 2000
                : 24 January 2000
                : 24 January 2000
                Categories
                Original Article

                Cell biology
                proteomics,nucleoporins,mass spectrometry,nuclear pore complex,nucleocytoplasmic transport

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