
pmid: 10884348
Transport across the nuclear membranes occurs through the nuclear pore complex (NPC), and is mediated by soluble transport factors including Ran, a small GTPase that is generally GDP-bound during import and GTP-bound for export. The dynamic nature of the NPC structure suggests a possible active role for it in driving translocation. Here we show that RanGTP but not RanGDP causes alterations of NPC structure when injected into the cytoplasm of Xenopus oocytes, including compaction of the NPC and extension of the cytoplasmic filaments. RanGTP caused accumulation of nucleoplasmin-gold along the length of extended cytoplasmic filaments, whereas RanGDP caused accumulation around the cytoplasmic rim of the NPC. This suggests a possible role for Ran in altering the conformation of the cytoplasmic filaments during transport.
Models, Molecular, 570, Cytoplasm, /dk/atira/pure/subjectarea/asjc/1300/1312, Nuclear Envelope, Recombinant Fusion Proteins, Transport, Guanosine Diphosphate, Xenopus laevis, Animals, Nucleoplasmins, Protein Structure, Quaternary, Binding Sites, Osmolar Concentration, Nuclear Proteins, Biological Transport, name=Molecular Biology, Phosphoproteins, Nuclear pore complex, Microscopy, Electron, Ran, Amino Acid Substitution, Oocytes, Gold, Guanosine Triphosphate, Protein Binding
Models, Molecular, 570, Cytoplasm, /dk/atira/pure/subjectarea/asjc/1300/1312, Nuclear Envelope, Recombinant Fusion Proteins, Transport, Guanosine Diphosphate, Xenopus laevis, Animals, Nucleoplasmins, Protein Structure, Quaternary, Binding Sites, Osmolar Concentration, Nuclear Proteins, Biological Transport, name=Molecular Biology, Phosphoproteins, Nuclear pore complex, Microscopy, Electron, Ran, Amino Acid Substitution, Oocytes, Gold, Guanosine Triphosphate, Protein Binding
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