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Ran alters nuclear pore complex conformation.
- Source :
-
Journal of molecular biology [J Mol Biol] 2000 Jul 14; Vol. 300 (3), pp. 519-29. - Publication Year :
- 2000
-
Abstract
- 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.<br /> (Copyright 2000 Academic Press.)
- Subjects :
- Amino Acid Substitution genetics
Animals
Binding Sites
Biological Transport
Cytoplasm chemistry
Cytoplasm metabolism
Cytoplasm ultrastructure
Gold
Guanosine Diphosphate metabolism
Guanosine Triphosphate metabolism
Microscopy, Electron
Models, Molecular
Nuclear Envelope chemistry
Nuclear Proteins metabolism
Nucleoplasmins
Oocytes
Osmolar Concentration
Phosphoproteins metabolism
Protein Binding
Protein Structure, Quaternary
Recombinant Fusion Proteins genetics
Recombinant Fusion Proteins metabolism
Xenopus laevis
ran GTP-Binding Protein genetics
Nuclear Envelope metabolism
Nuclear Envelope ultrastructure
ran GTP-Binding Protein metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0022-2836
- Volume :
- 300
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Journal of molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 10884348
- Full Text :
- https://doi.org/10.1006/jmbi.2000.3891