The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Extracellular Matrix Rigidity Promotes Invadopodia Activity
Open accessAbstract
Summary Invadopodia are actin-rich subcellular protrusions with associated proteases used by cancer cells to degrade extracellular matrix (ECM) [1]. Molecular components of invadopodia include branched actin assembly proteins, membrane trafficking proteins, signaling proteins and transmembrane proteinases[1]. Similar structures exist in nontransformed cells, such as osteoclasts and dendritic cells, but are generally called podosomes and are thought to be more involved in cell-matrix adhesion than invadopodia [2–4]. Despite intimate contact with their ECM substrates, it is unknown whether physical or chemical ECM signals regulate invadopodia function. Here, we report that ECM rigidity directly increases both the number and activity of invadopodia. Transduction of ECM rigidity signals depends on the cellular contractile apparatus [5–7], as inhibition of nonmuscle myosin II, myosin light chain kinase, and Rho kinase all abrogate invadopodia-associated ECM degradation. Whereas myosin IIA, IIB, and phosphorylated myosin light chain do not localize to invadopodia puncta, active phosphorylated forms of the mechanosensing proteins p130Cas (Cas) and focal adhesion kinase (FAK) are present in actively degrading invadopodia and the levels of phospho-Cas and phospho-FAK in invadopodia are sensitive to myosin inhibitors. Overexpression of Cas or FAK further enhances invadopodia activity in cells plated on rigid polyacrylamide substrates. Thus, in invasive cells, ECM rigidity signals lead to increased matrix-degrading activity at invadopodia, via a myosin II-FAK/Cas pathway. These data suggest a potential mechanism, via invadopodia, for the reported correlation of tissue density with cancer aggressiveness.
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Cites
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Force Sensing by Mechanical Extension of the Src Family Kinase Substrate p130Cas
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The matrix corroded: podosomes and invadopodia in extracellular matrix degradation
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Geiger, B., Spatz, J. P., & Bershadsky, A. D. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2593 · Cited by 2,543
Cellular functions of FAK kinases: insight into molecular mechanisms and novel functions
Schaller, M. D. (2010) · Journal of Cell Science · doi:10.1242/jcs.045112 · Cited by 599
Mechanoreciprocity in cell migration
van Helvert, S., Storm, C., & Friedl, P. (2018) · Nature Cell Biology · doi:10.1038/s41556-017-0012-0 · Cited by 587
3D collagen alignment limits protrusions to enhance breast cancer cell persistence
Riching, K. M., Cox, B. L., Salick, M. R., Pehlke, C., Riching, A. S., Ponik, S. M., Bass, B. R., Crone, W. C., Jiang, Y., Weaver, A. M., et al. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.10.035 · Cited by 446
Self-citationJanmey, P. A., Fletcher, D. A., & Reinhart-King, C. A. (2020) · Physiological Reviews · doi:10.1152/physrev.00013.2019 · Cited by 422
Metadata
- Authors
- Alexander, N. R., Branch, K. M., Parekh, A., Clark, E. S., Iwueke, I. C., Guelcher, S. A., & Weaver, A. M.
- Venue
- Current Biology
- Publisher
- Elsevier BV
- Published
- 2008-09
- Volume
- 18
- Issue
- 17
- Pages
- 1295-1299
- ISSN
- 0960-9822 (ISSN-L)
- OpenAlex
- W2153358370
- Cited by
- 317
- References
- 26
- FWCI
- 9.33
- Type
- journal article
- Language
- en
- Open access
- bronze
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