The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Role of Cofilin in Epidermal Growth Factor–Stimulated Actin Polymerization and Lamellipod Protrusion
Open accessAbstract
Stimulation of metastatic MTLn3 cells with epidermal growth factor (EGF) causes a rapid and transient increase in actin nucleation activity resulting from the appearance of free barbed ends at the extreme leading edge of extending lamellipods. To investigate the role of cofilin in EGF-stimulated actin polymerization and lamellipod extension in MTLn3 cells, we examined in detail the temporal and spatial distribution of cofilin relative to free barbed ends and characterized the actin dynamics by measuring the changes in the number of actin filaments. EGF stimulation triggers a transient increase in cofilin in the leading edge near the membrane, which is precisely cotemporal with the appearance of free barbed ends there. A deoxyribonuclease I binding assay shows that the number of filaments per cell increases by 1.5-fold after EGF stimulation. Detection of pointed ends in situ using deoxyribonuclease I binding demonstrates that this increase in the number of pointed ends is confined to the leading edge compartment, and does not occur within stress fibers or in the general cytoplasm. Using a light microscope severing assay, cofilin's severing activity was observed directly in cell extracts and shown to be activated after stimulation of the cells with EGF. Microinjection of function-blocking antibodies against cofilin inhibits the appearance of free barbed ends at the leading edge and lamellipod protrusion after EGF stimulation. These results support a model in which EGF stimulation recruits cofilin to the leading edge where its severing activity is activated, leading to the generation of short actin filaments with free barbed ends that participate in the nucleation of actin polymerization.
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Cites
Cell Migration: A Physically Integrated Molecular Process
Lauffenburger, D. A., & Horwitz, A. F. (1996) · Cell · doi:10.1016/s0092-8674(00)81280-5 · Cited by 3,915
Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex
Machesky, L. M., Mullins, R. D., Higgs, H. N., Kaiser, D. A., Blanchoin, L., May, R. C., Hall, M. E., & Pollard, T. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3739 · Cited by 773
Cited by
Cofilin Promotes Actin Polymerization and Defines the Direction of Cell Motility
Ghosh, M., Song, X., Mouneimne, G., Sidani, M., Lawrence, D. S., & Condeelis, J. S. (2004) · Science · doi:10.1126/science.1094561 · Cited by 657
Self-citationWang, W., Goswami, S., Lapidus, K., Wells, A. L., Wyckoff, J. B., Sahai, E., Singer, R. H., Segall, J. E., & Condeelis, J. S. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1136 · Cited by 455
Self-citationTHE GREAT ESCAPE: When Cancer Cells Hijack the Genes for Chemotaxis and Motility
Condeelis, J., Singer, R. H., & Segall, J. E. (2005) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.21.122303.120306 · Cited by 391
Self-citationHotulainen, P., Paunola, E., Vartiainen, M. K., & Lappalainen, P. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-07-0555 · Cited by 383
MILLARD, T. H., SHARP, S. J., & MACHESKY, L. M. (2004) · Biochemical Journal · doi:10.1042/bj20040176 · Cited by 278
Metadata
- Authors
- Chan, A. Y., Bailly, M., Zebda, N., Segall, J. E., & Condeelis, J. S.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2000-02-07
- Volume
- 148
- Issue
- 3
- Pages
- 531-542
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2033989449
- Cited by
- 243
- References
- 2
- FWCI
- 6.65
- Type
- journal article
- Language
- en
- Open access
- green
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- Chan, A. Y., Bailly, M., Zebda, N., Segall, J. E., & Condeelis, J. S. (2000). Role of Cofilin in Epidermal Growth Factor–Stimulated Actin Polymerization and Lamellipod Protrusion. The Journal of Cell Biology. https://doi.org/10.1083/jcb.148.3.531
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