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dc.contributor.authorKiseleva, Elena
dc.contributor.authorDrummond, Sheona P
dc.contributor.authorGoldberg, Martin W
dc.contributor.authorRutherford, Sandra A
dc.contributor.authorAllen, Terence D
dc.contributor.authorWilson, Katherine L
dc.date.accessioned2009-08-24T16:05:46Z
dc.date.available2009-08-24T16:05:46Z
dc.date.issued2004-05-15
dc.identifier.citationActin- and protein-4.1-containing filaments link nuclear pore complexes to subnuclear organelles in Xenopus oocyte nuclei. 2004, 117 (Pt 12):2481-90 J. Cell. Sci.en
dc.identifier.issn0021-9533
dc.identifier.pmid15128868
dc.identifier.doi10.1242/jcs.01098
dc.identifier.urihttp://hdl.handle.net/10541/78393
dc.description.abstractWe imaged the interiors of relatively intact Xenopus oocyte nuclei by field emission scanning electron microscopy (feSEM) and visualized a network of filaments that attach to nuclear pore complexes and extend throughout the nucleus. Within the nucleus, these 'pore-linked filaments' (PLFs) were embedded into spherical structures 100 nm to approximately 5 microm in diameter. A subset of spheres was identified as Cajal bodies by immuno-gold labeling; the rest were inferred to be nucleoli and snurposomes both of which are abundant in Xenopus oocyte nuclei. Most PLFs were independent of chromatin. The thickness of a typical PLF was 40 nm (range, approximately 12-100 nm), including the 4 nm chromium coat. PLFs located inside the nucleus merged, bundled and forked, suggesting architectural adaptability. The PLF network collapsed upon treatment with latrunculin A, which depolymerizes actin filaments. Jasplakinolide, which stabilizes actin filaments, produced PLFs with more open substructure including individual filaments with evenly-spaced rows of radially projecting short filaments. Immuno-gold labeling of untreated oocyte nuclei showed that actin and protein 4.1 each localized on PLFs. Protein 4.1-gold epitopes were spaced at approximately 120 nm intervals along filaments, and were often paired ( approximately 70 nm apart) at filament junctions. We suggest that protein 4.1 and actin contribute to the structure of a network of heterogeneous filaments that link nuclear pore complexes to subnuclear organelles, and discuss possible functions for PLFs in nuclear assembly and intranuclear traffic.
dc.language.isoenen
dc.subject.meshActins
dc.subject.meshAnimals
dc.subject.meshBicyclo Compounds, Heterocyclic
dc.subject.meshCell Nucleolus
dc.subject.meshCell Nucleus
dc.subject.meshChromatin
dc.subject.meshCoiled Bodies
dc.subject.meshCytoskeletal Proteins
dc.subject.meshDepsipeptides
dc.subject.meshFemale
dc.subject.meshImmunohistochemistry
dc.subject.meshMembrane Proteins
dc.subject.meshMicroscopy, Electron, Scanning
dc.subject.meshNuclear Pore
dc.subject.meshOocytes
dc.subject.meshProtein Binding
dc.subject.meshThiazoles
dc.subject.meshThiazolidines
dc.subject.meshXenopus
dc.titleActin- and protein-4.1-containing filaments link nuclear pore complexes to subnuclear organelles in Xenopus oocyte nuclei.en
dc.typeArticleen
dc.contributor.departmentDepartment of Structural Cell Biology, Paterson Institute for Cancer Research, Christie Hospital, Manchester, M20 9BX, UK.en
dc.identifier.journalJournal of Cell Scienceen
html.description.abstractWe imaged the interiors of relatively intact Xenopus oocyte nuclei by field emission scanning electron microscopy (feSEM) and visualized a network of filaments that attach to nuclear pore complexes and extend throughout the nucleus. Within the nucleus, these 'pore-linked filaments' (PLFs) were embedded into spherical structures 100 nm to approximately 5 microm in diameter. A subset of spheres was identified as Cajal bodies by immuno-gold labeling; the rest were inferred to be nucleoli and snurposomes both of which are abundant in Xenopus oocyte nuclei. Most PLFs were independent of chromatin. The thickness of a typical PLF was 40 nm (range, approximately 12-100 nm), including the 4 nm chromium coat. PLFs located inside the nucleus merged, bundled and forked, suggesting architectural adaptability. The PLF network collapsed upon treatment with latrunculin A, which depolymerizes actin filaments. Jasplakinolide, which stabilizes actin filaments, produced PLFs with more open substructure including individual filaments with evenly-spaced rows of radially projecting short filaments. Immuno-gold labeling of untreated oocyte nuclei showed that actin and protein 4.1 each localized on PLFs. Protein 4.1-gold epitopes were spaced at approximately 120 nm intervals along filaments, and were often paired ( approximately 70 nm apart) at filament junctions. We suggest that protein 4.1 and actin contribute to the structure of a network of heterogeneous filaments that link nuclear pore complexes to subnuclear organelles, and discuss possible functions for PLFs in nuclear assembly and intranuclear traffic.


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