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  • The Company of Biologists  (3)
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  • The Company of Biologists  (3)
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  • 1
    Online Resource
    Online Resource
    Actin filament turnover removes bundles from Drosophila bristle cells
    The Company of Biologists ; 2002
    In:  Journal of Cell Science Vol. 115, No. 3 ( 2002-02-01), p. 641-653
    Details
    In: Journal of Cell Science, The Company of Biologists, Vol. 115, No. 3 ( 2002-02-01), p. 641-653
    Abstract: Drosophila bristle cells form enormous extensions that are supported by equally impressive scaffolds of modular, polarized and crosslinked actin filament bundles. As the cell matures and support is taken over by the secreted cuticle, the actin scaffold is completely removed. This removal begins during cell elongation and proceeds via an orderly series of steps that operate on each module. Using confocal and electron microscopy, we found that the ∼500-filament modules are fractured longitudinally into 25-50-filament subbundles, indicating that module breakdown is the reverse of assembly. Time-lapse confocal analysis of GFP-decorated bundles in live cells showed that modules were shortened by subunit removal from filament barbed ends, again indicating that module breakdown is the reverse of assembly. Module shortening takes place at a fairly slow rate of ∼1μm/hour,implying that maximally crosslinked modules are not rapidly depolymerized. Barbed-end depolymerization was prevented with jasplakinolide and accelerated with cycloheximide, indicating that barbed-end maintenance requires continuous protein synthesis. Subbundle adhesion was lost in the presence of cytochalasin, indicating that continuous actin polymerization is required. Thus, these polarized actin filament bundles are dynamic structures that require continuous maintenance owing to protein and actin filament turnover. We propose that after cell elongation, maintenance falls behind turnover,resulting in the removal of this modular cytoskeleton.
    Type of Medium: Online Resource
    ISSN: 1477-9137 , 0021-9533
    URL: Article
    DOI: 10.1242/jcs.115.3.641
    Language: English
    Publisher: The Company of Biologists
    Publication Date: 2002
    detail.hit.zdb_id: 219171-4
    detail.hit.zdb_id: 1483099-1
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
  • 2
    Online Resource
    Online Resource
    Microvilli appear to represent the first step in actin bundle formation in Drosophila bristles
    The Company of Biologists ; 2004
    In:  Journal of Cell Science Vol. 117, No. 16 ( 2004-07-15), p. 3531-3538
    Details
    In: Journal of Cell Science, The Company of Biologists, Vol. 117, No. 16 ( 2004-07-15), p. 3531-3538
    Abstract: During bristle development the emerging bristle shaft, socket cell, and the apical surface of thoracic epithelial cells form tiny protuberances or pimples that contain electron-dense material located on the cytoplasmic surface of the pimple tip. In a few cases short actin filaments extend from this material into the cortical cytoplasm. When cultured in the presence of jasplakinolide, an agent that prevents filament disassembly, pimples elongate to form microvilli containing a core of crosslinked filaments. Emerging-bristle mutants delay cortical bundle formation and are aggregated by forked protein crossbridges. Using these mutants and enhancing core bundle formation with jasplakinolide we found that microvillar formation represents the first stage in the morphogenesis of much larger actin bundles in Drosophila bristle shaft cells. Evidence is presented showing that socket cells do not contain forked protein crossbridges, a fact that may explain why cortical bundles only appear in bristle shaft cells. Furthermore, as pimples and microvilli form in the absence of both forked and fascin crossbridges, we also conclude that neither of these crossbridges account for core bundle formation in microvilli, but there must exist a third, as yet unidentified crossbridge in this system. Immunocytochemisty suggested that this new crossbridge is not Drosophila villin. Finally, ultrastructural comparisons suggest that microspikes and microvilli form very differently.
    Type of Medium: Online Resource
    ISSN: 1477-9137 , 0021-9533
    URL: Article
    DOI: 10.1242/jcs.01215
    Language: English
    Publisher: The Company of Biologists
    Publication Date: 2004
    detail.hit.zdb_id: 219171-4
    detail.hit.zdb_id: 1483099-1
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
  • 3
    Online Resource
    Online Resource
    Actin filaments and microtubules play different roles during bristle elongation in Drosophila
    The Company of Biologists ; 2000
    In:  Journal of Cell Science Vol. 113, No. 7 ( 2000-04-01), p. 1255-1265
    Details
    In: Journal of Cell Science, The Company of Biologists, Vol. 113, No. 7 ( 2000-04-01), p. 1255-1265
    Abstract: Developing bristles in Drosophilapupae contain 7-11 bundles of crosslinked actin filaments and a large population of microtubules. During bristle growth the rate of cell elongation increases with bristle length. Thin section EM shows that bundle size is correlated with the amount of cytoplasm at all points along the bristle. Thus, as the bristle elongates and tapers, fewer actin filaments are used. To ensure penetration of inhibitors we isolated thoraces and cultured them in vitro; bristles elongate at rates identical to bristles growing in situ. Interestingly, inhibitors of actin filament assembly (cytochalasin D and latrunculin A) dramatically curtailed bristle elongation while a filament stabilizer (jasplakinolide) accelerated elongation. In contrast, inhibitors of microtubule dynamics (nocodazole, vinblastine, colchicine and taxol) did not affect bristle elongation. Surprisingly, the bristle microtubules are stable and do not turn over. Furthermore, the density of microtubules decreases as the bristle elongates. These two facts coupled with calculations and kinetics of elongation and the fact that the microtubules are short indicate that the microtubules are assembled early in development and then transported distally as the bristle grows. We conclude that actin assembly is crucial for bristle cell elongation and that microtubules must furnish other functions such as to provide bulk to the bristle cytoplasm as well as playing a role in vesicle transport.
    Type of Medium: Online Resource
    ISSN: 0021-9533 , 1477-9137
    URL: Article
    DOI: 10.1242/jcs.113.7.1255
    Language: English
    Publisher: The Company of Biologists
    Publication Date: 2000
    detail.hit.zdb_id: 219171-4
    detail.hit.zdb_id: 1483099-1
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
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