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First published online 5 May 2004
doi: 10.1242/jcs.01098
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Research Article |
1 Cancer Research UK, Department of Structural Cell Biology, Paterson Institute for Cancer Research, Christie Hospital, Wilmslow Road, Manchester, M20 9BX, UK
2 Department of Morphology and Function of Cell Structure, Institute of Cytology and Genetics, Russian Academy of Sciences, Novosibirsk-90, 630090, Russia
3 Department of Biological and Biomedical Sciences, Science Laboratories, University of Durham, South Road, Durham, DH1 3LE, UK
4 Department of Cell Biology, The Johns Hopkins School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA
* Author for correspondence (e-mail: klwilson{at}jhmi.edu)
Accepted 12 January 2004
We 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 
5 µm 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, 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 120 nm intervals along filaments, and were often paired (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.
Key words: Actin, Nucleocytoplasmic transport, Cajal bodies, Nuclear matrix, Nuclear pore complex, Nucleolus, Protein 4.1
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