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Article: Immobilization of the early secretory pathway by a virus glycoprotein that binds to microtubules

TitleImmobilization of the early secretory pathway by a virus glycoprotein that binds to microtubules
Authors
Issue Date2000
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/emboj/index.html
Citation
Embo Journal, 2000, v. 19 n. 23, p. 6465-6474 How to Cite?
AbstractMembrane trafficking from the endoplasmic reticulture (ER) to the Golgi complex is mediated by pleiomorphic carrier vesicles that are driven along microtubule tracks by the action of motor proteins. Here we describe how NSP4, a rotavirus membrane glycoprotein, binds to microtubules and blocks ER-to-Golgi trafficking in vivo. NSP4 accumulates in a post-ER, microtubule-associated membrane compartment and prevents targeting of vesicular stomatitis virus glycoprotein (VSV-G) at a pre-Golgi step. NSP4 also redistributes β-COP and ERGIC53, markers of a vesicular compartment that dynamically cycles between the ER and Golgi, to structures aligned along linear tracks radiating throughout the cytoplasm. This block in membrane trafficking is released when microtubules are depolymerized with nocodazole, indicating that vesicles containing NSP4 are tethered to the microtubule cytoskeleton. Disruption of microtubule-mediated membrane transport by a viral glycoprotein may represent a novel pathogenic mechanism and provides a new experimental tool for the dissection of early steps in exocytic transport.
Persistent Identifierhttp://hdl.handle.net/10722/162442
ISSN
2015 Impact Factor: 9.643
2015 SCImago Journal Rankings: 7.450
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorXu, Aen_US
dc.contributor.authorBellamy, ARen_US
dc.contributor.authorTaylor, JAen_US
dc.date.accessioned2012-09-05T05:19:57Z-
dc.date.available2012-09-05T05:19:57Z-
dc.date.issued2000en_US
dc.identifier.citationEmbo Journal, 2000, v. 19 n. 23, p. 6465-6474en_US
dc.identifier.issn0261-4189en_US
dc.identifier.urihttp://hdl.handle.net/10722/162442-
dc.description.abstractMembrane trafficking from the endoplasmic reticulture (ER) to the Golgi complex is mediated by pleiomorphic carrier vesicles that are driven along microtubule tracks by the action of motor proteins. Here we describe how NSP4, a rotavirus membrane glycoprotein, binds to microtubules and blocks ER-to-Golgi trafficking in vivo. NSP4 accumulates in a post-ER, microtubule-associated membrane compartment and prevents targeting of vesicular stomatitis virus glycoprotein (VSV-G) at a pre-Golgi step. NSP4 also redistributes β-COP and ERGIC53, markers of a vesicular compartment that dynamically cycles between the ER and Golgi, to structures aligned along linear tracks radiating throughout the cytoplasm. This block in membrane trafficking is released when microtubules are depolymerized with nocodazole, indicating that vesicles containing NSP4 are tethered to the microtubule cytoskeleton. Disruption of microtubule-mediated membrane transport by a viral glycoprotein may represent a novel pathogenic mechanism and provides a new experimental tool for the dissection of early steps in exocytic transport.en_US
dc.languageengen_US
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/emboj/index.htmlen_US
dc.relation.ispartofEMBO Journalen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAntineoplastic Agents - Pharmacologyen_US
dc.subject.meshAntineoplastic Agents, Phytogenic - Pharmacologyen_US
dc.subject.meshCos Cellsen_US
dc.subject.meshCell Lineen_US
dc.subject.meshCell Membrane - Metabolismen_US
dc.subject.meshCoatomer Protein - Metabolismen_US
dc.subject.meshCytoplasm - Metabolismen_US
dc.subject.meshCytoskeleton - Metabolismen_US
dc.subject.meshDna-Directed Rna Polymerasesen_US
dc.subject.meshDose-Response Relationship, Drugen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshEndoplasmic Reticulum - Metabolismen_US
dc.subject.meshExocytosisen_US
dc.subject.meshFluorescent Antibody Techniqueen_US
dc.subject.meshGlutathione Transferase - Metabolismen_US
dc.subject.meshGlycoproteins - Metabolismen_US
dc.subject.meshGlycoside Hydrolases - Pharmacologyen_US
dc.subject.meshGolgi Apparatus - Metabolismen_US
dc.subject.meshMacaca Mulattaen_US
dc.subject.meshMannose-Binding Lectinsen_US
dc.subject.meshMembrane Glycoproteinsen_US
dc.subject.meshMembrane Proteins - Metabolismen_US
dc.subject.meshMicroscopy, Confocalen_US
dc.subject.meshMicrotubules - Metabolismen_US
dc.subject.meshModels, Biologicalen_US
dc.subject.meshNocodazole - Pharmacologyen_US
dc.subject.meshPaclitaxel - Pharmacologyen_US
dc.subject.meshPlasmids - Metabolismen_US
dc.subject.meshPrecipitin Testsen_US
dc.subject.meshProtein Structure, Tertiaryen_US
dc.subject.meshProtein Transporten_US
dc.subject.meshRecombinant Fusion Proteins - Metabolismen_US
dc.subject.meshRotavirus - Metabolismen_US
dc.subject.meshTime Factorsen_US
dc.subject.meshTransfectionen_US
dc.subject.meshTubulin - Metabolismen_US
dc.subject.meshViral Envelope Proteins - Metabolismen_US
dc.subject.meshViral Nonstructural Proteins - Metabolismen_US
dc.titleImmobilization of the early secretory pathway by a virus glycoprotein that binds to microtubulesen_US
dc.typeArticleen_US
dc.identifier.emailXu, A:amxu@hkucc.hku.hken_US
dc.identifier.authorityXu, A=rp00485en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1093/emboj/19.23.6465-
dc.identifier.pmid11101519-
dc.identifier.scopuseid_2-s2.0-0034405490en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034405490&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume19en_US
dc.identifier.issue23en_US
dc.identifier.spage6465en_US
dc.identifier.epage6474en_US
dc.identifier.isiWOS:000165763800019-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridXu, A=7202655409en_US
dc.identifier.scopusauthoridBellamy, AR=7004515654en_US
dc.identifier.scopusauthoridTaylor, JA=24781484000en_US

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