The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Cortactin regulates cofilin and N-WASp activities to control the stages of invadopodium assembly and maturation
Open accessAbstract
Invadopodia are matrix-degrading membrane protrusions in invasive carcinoma cells. The mechanisms regulating invadopodium assembly and maturation are not understood. We have dissected the stages of invadopodium assembly and maturation and show that invadopodia use cortactin phosphorylation as a master switch during these processes. In particular, cortactin phosphorylation was found to regulate cofilin and Arp2/3 complex–dependent actin polymerization. Cortactin directly binds cofilin and inhibits its severing activity. Cortactin phosphorylation is required to release this inhibition so cofilin can sever actin filaments to create barbed ends at invadopodia to support Arp2/3-dependent actin polymerization. After barbed end formation, cortactin is dephosphorylated, which blocks cofilin severing activity thereby stabilizing invadopodia. These findings identify novel mechanisms for actin polymerization in the invadopodia of metastatic carcinoma cells and define four distinct stages of invadopodium assembly and maturation consisting of invadopodium precursor formation, actin polymerization, stabilization, and matrix degradation.
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Cites
Activation of Arp2/3 complex-mediated actin polymerization by cortactin
Uruno, T., Liu, J., Zhang, P., Fan, Y.-X., Egile, C., Li, R., Mueller, S. C., & Zhan, X. (2001) · Nature Cell Biology · doi:10.1038/35060051 · Cited by 568 · cited 3×
“Cortactin contains an N-terminal acidic (NTA) domain and a C-terminal SH3 domain that binds and activates the Arp2/3 complex (Weed et al., 2000; Uruno et al., 2001; Weaver et al., 2001) and N-WASp (Martinez-Quiles et al., 2004), respectively.”
BackgroundHow is actin polymerization nucleated in vivo?
Condeelis, J. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02008-6 · Cited by 258
Self-citationEGF-induced PIP2 hydrolysis releases and activates cofilin locally in carcinoma cells
van Rheenen, J., Song, X., van Roosmalen, W., Cammer, M., Chen, X., DesMarais, V., Yip, S.-C., Backer, J. M., Eddy, R. J., & Condeelis, J. S. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200706206 · Cited by 244
Self-citation
Cited by
Ridley, A. J. (2011) · Cell · doi:10.1016/j.cell.2011.06.010 · Cited by 956
ADF/Cofilin: a functional node in cell biology
Bernstein, B. W., & Bamburg, J. R. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.01.001 · Cited by 704
Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia
Schoumacher, M., Goldman, R. D., Louvard, D., & Vignjevic, D. M. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200909113 · Cited by 507
Matrix Metalloproteinases Shape the Tumor Microenvironment in Cancer Progression
Niland, S., Riscanevo, A. X., & Eble, J. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010146 · Cited by 503
Peltanova, B., Raudenska, M., & Masarik, M. (2019) · Molecular Cancer · doi:10.1186/s12943-019-0983-5 · Cited by 469
Metadata
- Authors
- Oser, M., Yamaguchi, H., Mader, C. C., Bravo-Cordero, J. J., Arias, M., Chen, X., DesMarais, V., van Rheenen, J., Koleske, A. J., & Condeelis, J.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2009-08-24
- Volume
- 186
- Issue
- 4
- Pages
- 571-587
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2112229259
- Cited by
- 369
- References
- 3
- FWCI
- 13.51
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Oser, M., Yamaguchi, H., Mader, C. C., Bravo-Cordero, J. J., Arias, M., Chen, X., DesMarais, V., van Rheenen, J., Koleske, A. J., & Condeelis, J. (2009). Cortactin regulates cofilin and N-WASp activities to control the stages of invadopodium assembly and maturation. Journal of Cell Biology. https://doi.org/10.1083/jcb.200812176
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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