2.50
Hdl Handle:
http://hdl.handle.net/10541/88046
Title:
Ran alters nuclear pore complex conformation.
Authors:
Goldberg, Martin W; Rutherford, Sandra A; Hughes, Mike F; Cotter, Laura A; Bagley, Steven; Kiseleva, Elena; Allen, Terence D; Clarke, Paul R
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.
Affiliation:
CRC Department of Structural Cell Biology, Paterson Institute for Cancer Research, Christie Hospital, Wilmslow Road, Manchester, M20 9BX, UK. mgoldberg@picr.man.ac.uk
Citation:
Ran alters nuclear pore complex conformation. 2000, 300 (3):519-29 J. Mol. Biol.
Journal:
Journal of Molecular Biology
Issue Date:
14-Jul-2000
URI:
http://hdl.handle.net/10541/88046
DOI:
10.1006/jmbi.2000.3891
PubMed ID:
10884348
Type:
Article
Language:
en
ISSN:
0022-2836
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorGoldberg, Martin Wen
dc.contributor.authorRutherford, Sandra Aen
dc.contributor.authorHughes, Mike Fen
dc.contributor.authorCotter, Laura Aen
dc.contributor.authorBagley, Stevenen
dc.contributor.authorKiseleva, Elenaen
dc.contributor.authorAllen, Terence Den
dc.contributor.authorClarke, Paul Ren
dc.date.accessioned2009-12-15T17:20:12Z-
dc.date.available2009-12-15T17:20:12Z-
dc.date.issued2000-07-14-
dc.identifier.citationRan alters nuclear pore complex conformation. 2000, 300 (3):519-29 J. Mol. Biol.en
dc.identifier.issn0022-2836-
dc.identifier.pmid10884348-
dc.identifier.doi10.1006/jmbi.2000.3891-
dc.identifier.urihttp://hdl.handle.net/10541/88046-
dc.description.abstractTransport 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.en
dc.language.isoenen
dc.subject.meshAmino Acid Substitution-
dc.subject.meshAnimals-
dc.subject.meshBinding Sites-
dc.subject.meshBiological Transport-
dc.subject.meshCytoplasm-
dc.subject.meshGold-
dc.subject.meshGuanosine Diphosphate-
dc.subject.meshGuanosine Triphosphate-
dc.subject.meshMicroscopy, Electron-
dc.subject.meshModels, Molecular-
dc.subject.meshNuclear Envelope-
dc.subject.meshNuclear Proteins-
dc.subject.meshOocytes-
dc.subject.meshOsmolar Concentration-
dc.subject.meshPhosphoproteins-
dc.subject.meshProtein Binding-
dc.subject.meshProtein Structure, Quaternary-
dc.subject.meshRecombinant Fusion Proteins-
dc.subject.meshXenopus laevis-
dc.subject.meshran GTP-Binding Protein-
dc.titleRan alters nuclear pore complex conformation.en
dc.typeArticleen
dc.contributor.departmentCRC Department of Structural Cell Biology, Paterson Institute for Cancer Research, Christie Hospital, Wilmslow Road, Manchester, M20 9BX, UK. mgoldberg@picr.man.ac.uken
dc.identifier.journalJournal of Molecular Biologyen

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