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dc.contributor.authorWalther, Tobias C
dc.contributor.authorFornerod, Maarten
dc.contributor.authorPickersgill, Helen
dc.contributor.authorGoldberg, Martin W
dc.contributor.authorAllen, Terence D
dc.contributor.authorMattaj, Iain W
dc.date.accessioned2009-11-06T14:52:12Z
dc.date.available2009-11-06T14:52:12Z
dc.date.issued2001-10-15
dc.identifier.citationThe nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins. 2001, 20 (20):5703-14 EMBO J.en
dc.identifier.issn0261-4189
dc.identifier.pmid11598013
dc.identifier.doi10.1093/emboj/20.20.5703
dc.identifier.urihttp://hdl.handle.net/10541/85549
dc.description.abstractThe nuclear pore complex (NPC) is a large proteinaceous structure through which bidirectional transport of macromolecules across the nuclear envelope (NE) takes place. Nup153 is a peripheral NPC component that has been implicated in protein and RNP transport and in the interaction of NPCs with the nuclear lamina. Here, Nup153 is localized by immunogold electron microscopy to a position on the nuclear ring of the NPC. Nuclear reconstitution is used to investigate the role of Nup153 in nucleo- cytoplasmic transport and NPC architecture. NPCs assembled in the absence of Nup153 lacked several nuclear basket components, were unevenly distributed in the NE and, unlike wild-type NPCs, were mobile within the NE. Importin alpha/beta-mediated protein import into the nucleus was strongly reduced in the absence of Nup153, while transportin-mediated import was unaffected. This was due to a reduction in import complex translocation rather than to defective receptor recycling. Our results therefore reveal functions for Nup153 in NPC assembly, in anchoring NPCs within the NE and in mediating specific nuclear import events.
dc.language.isoenen
dc.subject.meshAnimals
dc.subject.meshCattle
dc.subject.meshFemale
dc.subject.meshHeterogeneous-Nuclear Ribonucleoproteins
dc.subject.meshHumans
dc.subject.meshImmunohistochemistry
dc.subject.meshKaryopherins
dc.subject.meshMacromolecular Substances
dc.subject.meshMale
dc.subject.meshMicroscopy, Immunoelectron
dc.subject.meshNuclear Pore
dc.subject.meshNuclear Pore Complex Proteins
dc.subject.meshNuclear Proteins
dc.subject.meshOocytes
dc.subject.meshPhosphoproteins
dc.subject.meshProtein Transport
dc.subject.meshRecombinant Fusion Proteins
dc.subject.meshRibonucleoproteins
dc.subject.meshSerum Albumin, Bovine
dc.subject.meshXenopus laevis
dc.titleThe nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins.en
dc.typeArticleen
dc.contributor.departmentEuropean Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.en
dc.identifier.journalThe EMBO Journalen
html.description.abstractThe nuclear pore complex (NPC) is a large proteinaceous structure through which bidirectional transport of macromolecules across the nuclear envelope (NE) takes place. Nup153 is a peripheral NPC component that has been implicated in protein and RNP transport and in the interaction of NPCs with the nuclear lamina. Here, Nup153 is localized by immunogold electron microscopy to a position on the nuclear ring of the NPC. Nuclear reconstitution is used to investigate the role of Nup153 in nucleo- cytoplasmic transport and NPC architecture. NPCs assembled in the absence of Nup153 lacked several nuclear basket components, were unevenly distributed in the NE and, unlike wild-type NPCs, were mobile within the NE. Importin alpha/beta-mediated protein import into the nucleus was strongly reduced in the absence of Nup153, while transportin-mediated import was unaffected. This was due to a reduction in import complex translocation rather than to defective receptor recycling. Our results therefore reveal functions for Nup153 in NPC assembly, in anchoring NPCs within the NE and in mediating specific nuclear import events.


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