Actions of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone.
Open accessAbstract
Actions of cytochalasin B (CB) on cytoskeletons and motility of growth cones from cultured Aplysia neurons were studied using a rapid flow perfusion chamber and digital video light microscopy. Living growth cones were observed using differential interference contrast optics and were also fixed at various time points to assay actin filament (F-actin) and microtubule distributions. Treatment with CB reversibly blocked motility and eliminated most of the phalloidin-stainable F-actin from the leading lamella. The loss of F-actin was nearly complete within 2-3 min of CB application and was largely reversed within 5-6 min of CB removal. The loss and recovery of F-actin were found to occur with a very distinctive spatial organization. Within 20-30 s of CB application, F-actin networks receded from the entire peripheral margin of the lamella forming a band devoid of F-actin. This band widened as F-actin receded at rates of 3-6 microns/min. Upon removal of CB, F-actin began to reappear within 20-30 s. The initial reappearance of F-actin took two forms: a coarse isotropic matrix of F-actin bundles throughout the lamella, and a denser matrix along the peripheral margin. The denser peripheral matrix then expanded in width, extending centrally to replace the coarse matrix at rates again between 3-6 microns/min. These results suggest that actin normally polymerizes at the leading edge and then flows rearward at a rate between 3-6 microns/min. CB treatment was also observed to alter the distribution of microtubules, assayed by antitubulin antibody staining. Normally, microtubules are restricted to the neurite shaft and a central growth cone domain. Within approximately 5 min after CB application, however, microtubules began extending into the lamellar region, often reaching the peripheral margin. Upon removal of CB, the microtubules were restored to their former central localization. The timing of these microtubule redistributions is consistent with their being secondary to effects of CB on lamellar F-actin.
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Low concentrations of AAIs (0.01-1 μM) are similar to those shown previously to alter actin filament organization in cultured cells, prevent lamellipodial ruffling in fibroblasts, inhibit motility and retrograde flow in neuronal growth cones, and arrest dendritic spine motility in hippocampal neurons.
“The concentrations of latrunculin A and cytochalasins used here (0.01–1 μM) are similar to those that have been shown previously to alter actin filament organization in cultured cells, prevent lamellipodial ruffling in fibroblasts, inhibit motility and retrograde flow in neuronal growth cones, and arrest dendritic spine motility in hippocampal neurons (3, 4, 7, 10).”
From Dynamic actin filaments are required for stable long-term potentiation (LTP) in area CA1 of the hippocampus (2000) · cites this paper as [7]
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Cites
Effects of cytochalasin and phalloidin on actin.
Cooper, J. A. (1987) · The Journal of cell biology · doi:10.1083/jcb.105.4.1473 · Cited by 2,009 · see citing works
Microfilaments in Cellular and Developmental Processes
Wessells, N. K., Spooner, B. S., Ash, J. F., Bradley, M. O., Ludueña, M. A., Taylor, E. L., Wrenn, J. T., & Yamada, K. M. (1971) · Science · doi:10.1126/science.171.3967.135 · Cited by 1,552 · see citing works
ACTIN AND ACTIN-BINDING PROTEINS. A CRITICAL EVALUATION OF MECHANISMS AND FUNCTIONS
Pollard, T. D., & Cooper, J. A. (1986) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.55.070186.005011 · Cited by 1,505 · see citing works
Fluorescent phallotoxin, a tool for the visualization of cellular actin.
Wulf, E., Deboben, A., Bautz, F. A., Faulstich, H., & Wieland, T. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.9.4498 · Cited by 789 · see citing works
ULTRASTRUCTURE AND FUNCTION OF GROWTH CONES AND AXONS OF CULTURED NERVE CELLS
Yamada, K. M., Spooner, B. S., & Wessells, N. K. (1971) · The Journal of Cell Biology · doi:10.1083/jcb.49.3.614 · Cited by 767 · see citing works
Mechanism of action of cytochalasin B on actin
MacLean-Fletcher, S. (1980) · Cell · doi:10.1016/0092-8674(80)90619-4 · Cited by 755 · see citing works
Actin polymerization and its regulation by proteins from nonmuscle cells.
Korn, E. D. (1982) · Physiological Reviews · doi:10.1152/physrev.1982.62.2.672 · Cited by 741 · see citing works
Mooseker, M. S., & Tilney, L. G. (1975) · The Journal of Cell Biology · doi:10.1083/jcb.67.3.725 · Cited by 624 · see citing works
Bray, D., & White, J. G. (1988) · Science · doi:10.1126/science.3277283 · Cited by 582 · see citing works
Barak, L. S., Yocum, R. R., Nothnagel, E. A., et al. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.2.980 · Cited by 440 · see citing works
Flanagan, M. D., & Lin, S. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86105-7 · Cited by 437 · see citing works
A new hypothesis of contact guidance in tissue cells
Dunn, G., & Heath, J. P. (1976) · Experimental Cell Research · doi:10.1016/0014-4827(76)90405-5 · Cited by 425 · see citing works
ALLEN, R. D., Allen, N. S., & Travis, J. L. (1981) · Cell Motility · doi:10.1002/cm.970010303 · Cited by 419 · see citing works
Bentley, D., & Toroian‐Raymond, A. (1986) · Nature · doi:10.1038/323712a0 · Cited by 378 · see citing works
The locomotion of fibroblasts in culture
Abercrombie, M., Heaysman, J. E. M., & Pegrum, S. M. (1970) · Experimental Cell Research · doi:10.1016/0014-4827(70)90570-7 · Cited by 349 · see citing works
Phosphorylation of microtubule-associated proteins regulates their interaction with actin filaments.
Selden, S. C., & Pollard, T. D. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32333-0 · Cited by 314 · see citing works
Inoué, S. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.89.2.346 · Cited by 308 · see citing works
Actin polymerization. The mechanism of action of cytochalasin D.
Goddette, D. W., & Frieden, C. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66662-1 · Cited by 275 · see citing works
Dynamic and stable populations of microtubules in cells.
Schulze, E., & Kirschner, M. W. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.104.2.277 · Cited by 268 · see citing works
Mechanism of action of cytochalasin: evidence that it binds to actin filament ends.
Brown, S. S., & Spudich, J. A. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.88.3.487 · Cited by 262 · see citing works
Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation.
Lin, D., Tobin, K. D., Grumet, M., et al. (1980) · The Journal of Cell Biology · doi:10.1083/jcb.84.2.455 · Cited by 259 · see citing works
Biochemical Studies on the Mode of Action of Cytochalasin B
Lin, S., & Spudich, J. A. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)79884-4 · Cited by 254 · see citing works
An actin-binding protein from Acanthamoeba regulates actin filament polymerization and interactions
Isenberg, G., Aebi, U., & Pollard, T. D. (1980) · Nature · doi:10.1038/288455a0 · Cited by 244 · see citing works
ACTION OF CYTOCHALASIN D ON CELLS OF ESTABLISHED LINES
Miranda, A. F., Godman, G. C., Deitch, A. D., et al. (1974) · The Journal of Cell Biology · doi:10.1083/jcb.61.2.481 · Cited by 241 · see citing works
Cytochalasin B and the structure of actin gels
Hartwig, J. H., & Stossel, T. P. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90366-8 · Cited by 236 · see citing works
Tension and compression in the cytoskeleton of PC 12 neurites.
Joshi, H. C., Chu, D., Buxbaum, R. E., & Heidemann, S. R. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.3.697 · Cited by 224 · see citing works
Letourneau, P. C. (1983) · The Journal of Cell Biology · doi:10.1083/jcb.97.4.963 · Cited by 214 · see citing works
Weber, K., Rathke, P. C., Osborn, M., et al. (1976) · Experimental Cell Research · doi:10.1016/0014-4827(76)90044-6 · Cited by 211 · see citing works
Letourneau, P. C., Shattuck, T. A., & Ressler, A. H. (1987) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970080302 · Cited by 207 · see citing works
Casella, J. F., Maack, D. J., & Lin, S. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67474-5 · Cited by 186 · see citing works
Forscher, P., Kaczmarek, L. K., Buchanan, J., et al. (1987) · Journal of Neuroscience · doi:10.1523/jneurosci.07-11-03600.1987 · Cited by 177 · see citing works
Self-citationCorrelation between growth form and movement and their dependence on neuronal age
Argiro, V., Bunge, M., & Johnson, M. (1984) · Journal of Neuroscience · doi:10.1523/jneurosci.04-12-03051.1984 · Cited by 147 · see citing works
Bonder, E. M., Fishkind, D. J., & Mooseker, M. S. (1983) · Cell · doi:10.1016/0092-8674(83)90382-3 · Cited by 138 · see citing works
Actin filaments elongate from their membrane-associated ends
Tilney, L. G., Bonder, E. M., & DeRosier, D. J. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.90.2.485 · Cited by 135 · see citing works
Letourneau, P. C. (1981) · Developmental Biology · doi:10.1016/0012-1606(81)90240-2 · Cited by 125 · see citing works
Cytochalasin B slows but does not prevent monomer addition at the barbed end of the actin filament.
Bonder, E. M., & Mooseker, M. S. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.102.1.282 · Cited by 104 · see citing works
OSTER, G. F. (1984) · PubMed · Cited by 103 · see citing works
Mooseker, M. S., Pollard, T. D., & Wharton, K. A. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.95.1.223 · Cited by 96 · see citing works
Cytochalasin B inhibits actin-related gelation of HeLa cell extracts.
Weihing, R. R. (1976) · The Journal of Cell Biology · doi:10.1083/jcb.71.1.303 · Cited by 96 · see citing works
Actin cytoskeleton of spread fibroblasts appears to assemble at the cell edges
Svitkina, T. M., Neyfakh, A. A., & Bershadsky, A. D. (1986) · Journal of Cell Science · doi:10.1242/jcs.82.1.235 · Cited by 82 · see citing works
Bonder, E. M., & Mooseker, M. (1983) · The Journal of Cell Biology · doi:10.1083/jcb.96.4.1097 · Cited by 79 · see citing works
Actin and Actin-Binding Proteins. A Critical Evaluation of Mechanisms and Functions
Pollard, T. D. (1986) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.55.1.987 · Cited by 73 · see citing works
Direct evidence for microfilament-mediated capping of surface receptors on crawling fibroblasts
Heath, J. P. (1983) · Nature · doi:10.1038/302532a0 · Cited by 69 · see citing works
Subcellular compartmentalization by local differentiation of cytoplasmic structure
Luby‐Phelps, K., & Taylor, D. L. (1988) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970100107 · Cited by 59 · see citing works
Red Cell Biochemical Anatomy and Membrane Properties
Chasis, J. A., & Shohet, S. B. (1987) · Annual Review of Physiology · doi:10.1146/annurev.ph.49.030187.001321 · Cited by 57 · see citing works
Spectroscopic evidence for the interaction of phalloidin with actin
Wieland, T., Vries, J. X. D., Schäfer, A. J., et al. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)81071-4 · Cited by 54 · see citing works
Maruyama, K., Hartwig, J. H., & Stossel, T. P. (1980) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(80)90146-4 · Cited by 46 · see citing works
Back, N., Lajtha, Á., Lambris, J. D., et al. (2007) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-76715-4 · Cited by 39 · see citing works
Biology of the Nerve Growth Cone
Gordon‐Weeks, P. R. (1986) · Trends in Neurosciences · doi:10.1016/0166-2236(86)90100-1 · Cited by 26 · see citing works
Biology of the nerve growth cone
Kater, S. B., & Letourneau, P. C. (1985) · Medical Entomology and Zoology · Cited by 24 · see citing works
Red Cell Biochemical Anatomy And Membrane Properties
Chasis, J. (1987) · Annual Review of Physiology · doi:10.1146/annurev.physiol.49.1.237 · Cited by 6 · see citing works
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Kozminski, K. G., Johnson, K. A., Forscher, P., & Rosenbaum, J. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.12.5519 · Cited by 1,007 · see citing works
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Fischer, M., Kaech, S., Knutti, D., & Matus, A. (1998) · Neuron · doi:10.1016/s0896-6273(00)80467-5 · Cited by 905 · see citing works
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Luo, L. (2002) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.18.031802.150501 · Cited by 658 · see citing works
Spector, I., Shochet, N. R., Blasberger, D., & Kashman, Y. (1989) · Cell Motility · doi:10.1002/cm.970130302 · Cited by 580 · see citing works
Actin- and myosin-driven movement of viruses along filopodia precedes their entry into cells
Lehmann, M. J., Sherer, N. M., Marks, C. B., Pypaert, M., & Mothes, W. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200503059 · Cited by 403 · see citing works
Krucker, T., Siggins, G. R., & Halpain, S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100139797 · Cited by 374 · see citing works
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Blanquie, O., & Bradke, F. (2018) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2018.02.024 · Cited by 189 · see citing works
Ferreira, A., Kincaid, R., & Kosik, K. S. (1993) · Molecular Biology of the Cell · doi:10.1091/mbc.4.12.1225 · Cited by 110 · see citing works
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- Authors
- Forscher, P., & Smith, S. J.
- Affiliations
- Howard Hughes Medical Institute (US)
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1988-10-01
- Volume
- 107
- Issue
- 4
- Pages
- 1505-1516
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2115246
- OpenAlex
- W1992835639
- Cited by
- 854
- References
- 51
- Citations by year
- 2026: 8 · 2025: 3 · 2024: 7 · 2023: 10 · 2022: 16 · 2021: 13 · 2020: 10 · 2019: 16 · 2018: 15 · 2017: 11 · 2016: 20 · 2015: 14 · 2014: 19 · 2013: 18 · 2012: 24
- FWCI
- 13.23
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- cytochalasin B, F-actin, microtubules, growth cones, growth cone motility, Aplysia neurons, F-actin polymerization, actin flow, cytoskeletal organization, neurite outgrowth
- MeSH terms
- Actins, Animals, Aplysia, Cell Movement, Cells, Cultured, Cytochalasins, Cytoskeleton, Image Processing, Computer-Assisted, Actin Cytoskeleton, Microtubules, Neurons, Polymers, Time Factors, Video Recording, In Vitro Techniques
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