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  • 1
    Online Resource
    Online Resource
    Kinetic-structural analysis of neuronal growth cone veil motility
    The Company of Biologists ; 2007
    In:  Journal of Cell Science Vol. 120, No. 6 ( 2007-03-15), p. 1113-1125
    Details
    In: Journal of Cell Science, The Company of Biologists, Vol. 120, No. 6 ( 2007-03-15), p. 1113-1125
    Abstract: Neuronal growth cone advance was investigated by correlative light and electron microscopy carried out on chick dorsal root ganglion cells. Advance was analyzed in terms of the two principal organelles responsible for protrusive motility in the growth cone – namely, veils and filopodia. Veils alternated between rapid phases of protrusion and retraction. Electron microscopy revealed characteristic structural differences between the phases. Our results provide a significant advance in three respects: first, protruding veils are comprised of a densely branched network of actin filaments that is lamellipodial in appearance and includes the Arp2/3 complex. On the basis of this structural and biomarker evidence, we infer that the dendritic nucleation and/or array-treadmilling mechanism of protrusive motility is conserved in veil protrusion of growth cones as in the motility of fibroblasts; second, retracting veils lack dendritic organization but contain a sparse network of long filaments; and third, growth cone filopodia have the capacity to nucleate dendritic networks along their length, a property consistent with veil formation seen at the light microscopic level but not previously understood in supramolecular terms. These elements of veil and filopodial organization, when taken together, provide a conceptual framework for understanding the structural basis of growth cone advance.
    Type of Medium: Online Resource
    ISSN: 1477-9137 , 0021-9533
    URL: Article
    DOI: 10.1242/jcs.03384
    Language: English
    Publisher: The Company of Biologists
    Publication Date: 2007
    detail.hit.zdb_id: 219171-4
    detail.hit.zdb_id: 1483099-1
    SSG: 12
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  • 2
    Online Resource
    Online Resource
    A Rickettsia WASP-like protein activates the Arp2/3 complex and mediates actin-based motility : Rickettsia RickA activates the Arp2/3 complex
    Hindawi Limited ; 2004
    In:  Cellular Microbiology Vol. 6, No. 8 ( 2004-07-05), p. 761-769
    Details
    In: Cellular Microbiology, Hindawi Limited, Vol. 6, No. 8 ( 2004-07-05), p. 761-769
    Type of Medium: Online Resource
    ISSN: 1462-5814 , 1462-5822
    URL: Issue
    URL: Article
    DOI: 10.1111/cmi.2004.6.issue-8
    DOI: 10.1111/j.1462-5822.2004.00402.x
    Language: English
    Publisher: Hindawi Limited
    Publication Date: 2004
    detail.hit.zdb_id: 2019990-9
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    Antagonism between Ena/VASP Proteins and Actin Filament Capping Regulates Fibroblast Motility
    Elsevier BV ; 2002
    In:  Cell Vol. 109, No. 4 ( 2002-05), p. 509-521
    Details
    In: Cell, Elsevier BV, Vol. 109, No. 4 ( 2002-05), p. 509-521
    Type of Medium: Online Resource
    ISSN: 0092-8674
    URL: Article
    DOI: 10.1016/S0092-8674(02)00731-6
    RVK:
    XA 36269
    RVK:
    WA 15000
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2002
    detail.hit.zdb_id: 187009-9
    detail.hit.zdb_id: 2001951-8
    SSG: 12
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  • 4
    Online Resource
    Online Resource
    Mechanism of filopodia initiation by reorganization of a dendritic network
    Rockefeller University Press ; 2003
    In:  The Journal of Cell Biology Vol. 160, No. 3 ( 2003-02-03), p. 409-421
    Details
    In: The Journal of Cell Biology, Rockefeller University Press, Vol. 160, No. 3 ( 2003-02-03), p. 409-421
    Abstract: Afilopodium protrudes by elongation of bundled actin filaments in its core. However, the mechanism of filopodia initiation remains unknown. Using live-cell imaging with GFP-tagged proteins and correlative electron microscopy, we performed a kinetic-structural analysis of filopodial initiation in B16F1 melanoma cells. Filopodial bundles arose not by a specific nucleation event, but by reorganization of the lamellipodial dendritic network analogous to fusion of established filopodia but occurring at the level of individual filaments. Subsets of independently nucleated lamellipodial filaments elongated and gradually associated with each other at their barbed ends, leading to formation of cone-shaped structures that we term Λ-precursors. An early marker of initiation was the gradual coalescence of GFP-vasodilator-stimulated phosphoprotein (GFP-VASP) fluorescence at the leading edge into discrete foci. The GFP-VASP foci were associated with Λ-precursors, whereas Arp2/3 was not. Subsequent recruitment of fascin to the clustered barbed ends of Λ-precursors initiated filament bundling and completed formation of the nascent filopodium. We propose a convergent elongation model of filopodia initiation, stipulating that filaments within the lamellipodial dendritic network acquire privileged status by binding a set of molecules (including VASP) to their barbed ends, which protect them from capping and mediate association of barbed ends with each other.
    Type of Medium: Online Resource
    ISSN: 1540-8140 , 0021-9525
    URL: Article
    DOI: 10.1083/jcb.200210174
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 2003
    detail.hit.zdb_id: 1421310-2
    SSG: 12
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  • 5
    Online Resource
    Online Resource
    Microtubule-targeting-dependent reorganization of filopodia
    The Company of Biologists ; 2007
    In:  Journal of Cell Science Vol. 120, No. 7 ( 2007-04-01), p. 1235-1244
    Details
    In: Journal of Cell Science, The Company of Biologists, Vol. 120, No. 7 ( 2007-04-01), p. 1235-1244
    Abstract: Interaction between the microtubule system and actin cytoskeleton has emerged as a fundamental process required for spatial regulation of cell protrusion and retraction activities. In our current studies, analysis of digital fluorescence images revealed targeting of microtubules to filopodia in B16F1 melanoma cells and fibroblasts. We investigated the functional consequence of targeting on filopodia reorganization and examined mechanisms by which microtubules may be guided to, or interact with, filopodia. Live cell imaging studies show that targeting events in lamellipodia wings temporally correlated with filopodia turning toward the lamellipodium midline and with filopodia merging. Rapid uncoupling of targeting with nocodazole decreased filopodia merging events and increased filopodia density. Total internal reflection fluorescence microscopy identified microtubules near the ventral surface and upward movement of targeted filopodia. The role of adhesion sites and microtubule plus-end proteins in targeting was investigated. Correlation of adhesion sites with microtubule targeting to filopodia was not observed and depletion of microtubule plus-end proteins did not significantly alter targeting frequency. We propose that microtubules target filopodia, independent of focal adhesions and plus-end proteins, causing filopodia movement and microtubules regulate filopodia density in lamellipodia wings through filopodia merging events.
    Type of Medium: Online Resource
    ISSN: 1477-9137 , 0021-9533
    URL: Article
    DOI: 10.1242/jcs.003913
    Language: English
    Publisher: The Company of Biologists
    Publication Date: 2007
    detail.hit.zdb_id: 219171-4
    detail.hit.zdb_id: 1483099-1
    SSG: 12
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  • 6
    Online Resource
    Online Resource
    Orientational Order of the Lamellipodial Actin Network as Demonstrated in Living Motile Cells
    American Society for Cell Biology (ASCB) ; 2003
    In:  Molecular Biology of the Cell Vol. 14, No. 11 ( 2003-11), p. 4667-4675
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 14, No. 11 ( 2003-11), p. 4667-4675
    Abstract: Lamellipodia of crawling cells represent both the motor for cell advance and the primary building site for the actin cytoskeleton. The organization of actin in the lamellipodium reflects actin dynamics and is of critical importance for the mechanism of cell motility. In previous structural studies, the lamellipodial actin network was analyzed primarily by electron microscopy (EM). An understanding of lamellipodial organization would benefit significantly if the EM data were complemented and put into a kinetic context by establishing correspondence with structural features observable at the light microscopic level in living cells. Here, we use an enhanced phase contrast microscopy technique to visualize an apparent long-range diagonal actin meshwork in the advancing lamellipodia of living cells. Visualization of this meshwork permitted a correlative light and electron microscopic approach that validated the underlying organization of lamellipodia. The linear features in the light microscopic meshwork corresponded to regions of greater actin filament density. Orientation of features was analyzed quantitatively and compared with the orientation of actin filaments at the EM level. We infer that the light microscopic meshwork reflects the orientational order of actin filaments which, in turn, is related to their branching angle.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e02-10-0630
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2003
    detail.hit.zdb_id: 1474922-1
    SSG: 12
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