Regulation of cancer invasion by reactive oxygen species and Tks family scaffold proteins

Science Signaling

Volumn 2, Issue 88, 2009, Pages

  Weaver, Alissa M ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; PROTEIN TYROSINE KINASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SCAFFOLD PROTEIN; PHOSPHOPROTEIN; SH3PXD2A PROTEIN, HUMAN; TKS4 PROTEIN, MOUSE; VESICULAR TRANSPORT ADAPTOR PROTEIN;

CANCER INVASION; CELL ADHESION; CELL FUNCTION; CELL STRUCTURE; ENZYME MECHANISM; EXTRACELLULAR MATRIX; INVADOPODIA; PODOSOME; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION; SHORT SURVEY; SIGNAL TRANSDUCTION; ANIMAL; ARTICLE; CELL SURFACE; HUMAN; METABOLISM; NEOPLASM; PATHOLOGY; PHYSIOLOGY;

ADAPTOR PROTEINS, VESICULAR TRANSPORT; ANIMALS; CELL SURFACE EXTENSIONS; HUMANS; NADPH OXIDASE; NEOPLASM INVASIVENESS; NEOPLASMS; PHOSPHOPROTEINS; REACTIVE OXYGEN SPECIES;

EID: 73949147048     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.288pe56     Document Type: Short Survey

References (26)

1. K. Bedard, K. H. Krause, The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology. Physiol. Rev. 87, 245-313 (2007).
2. M. G. Binker, A. A. Binker-Cosen, D. Richards, B. Oliver, L. I. Cosen-Binker, EGF promotes invasion by PANC-1 cells through Rac1/ROS-dependent secretion and activation of MMP-2. Biochem. Biophys. Res. Commun. 379, 445-450 (2009).
3. D. Ferraro, S. Corso, E. Fasano, E. Panieri, R. Santangelo, S. Borrello, S. Giordano, G. Pani, T. Galeotti, Pro-metastatic signaling by c-Met through RAC-1 and reactive oxygen species (ROS). Oncogene 25, 3689-3698 (2006).
4. D. Gianni, B. Bohl, S. A. Courtneidge, G. M. Bokoch, The involvement of the tyrosine kinase c-Src in the regulation of reactive oxygen species generation mediated by NADPH oxidase-1. Mol. Biol. Cell 19, 2984-2994 (2008).
5. J. Mitsushita, J. D. Lambeth, T. Kamata, The superoxide- generating oxidase Nox1 is functionally required for Ras oncogene transformation. Cancer Res. 64, 3580-3585 (2004).
6. W. S.Wu, The signaling mechanism of ROS in tumor progression. Cancer Metastasis Rev. 25, 695-705 (2006).
7. B. Diaz, G. Shani, I. Pass, D. Anderson, M. Quintavalle, S. A. Courtneidge, Tks5-dependent, Noxmediated generation of reactive oxygen species is necessary for invadopodia formation. Sci. Signal. 2, ra53 (2009).
8. phox-related organizers regulate NADPH oxidase 1 (Nox1) activity and localization. Sci. Signal. 2, ra54 (2009).
9. A. M.Weaver, Invadopodia: Specialized cell structures for cancer invasion. Clin. Exp. Metastasis 23, 97-105 (2006).
10. A. M. Weaver, Invadopodia. Curr. Biol. 18, R362-R364 (2008).
11. E. T. Bowden, M. Barth, D. Thomas, R. I. Glazer, S. C. Mueller, An invasion-related complex of cortactin, paxillin and PKCmu associates with invadopodia at sites of extracellular matrix degradation. Oncogene 18, 4440-4449 (1999).
12. P. J. Coopman, M. T. Do, E. W. Thompson, S. C. Mueller, Phagocytosis of cross-linked gelatin matrix by human breast carcinoma cells correlates with their invasive capacity. Clin. Cancer Res. 4, 507-515 (1998).
13. E. W. Thompson, S. Paik, N. Brünner, C. L. Sommers, G. Zugmaier, R. Clarke, T. B. Shima, J. Torri, S. Donahue, M. E. Lippman, G. R. Martin, R. B. Dickson, Association of increased basement membrane invasiveness with absence of estrogen receptor and expression of vimentin in human breast cancer cell lines. J. Cell. Physiol. 150, 534-544 (1992).
14. M. Gimona, R. Buccione, S. A. Courtneidge, S. Linder, Assembly and biological role of podosomes and invadopodia. Curr. Opin. Cell Biol. 20, 235-241 (2008).
15. M. D. Buschman, P. A. Bromann, P. Cejudo-Martin, F. Wen, I. Pass, S. A. Courtneidge, The novel adaptor protein Tks4 (SH3PXD2B) is required for functional podosome formation. Mol. Biol. Cell 20, 1302-1311 (2009).
16. D. F. Seals, E. F. Azucena Jr., I. Pass, L. Tesfay, R. Gordon, M. Woodrow, J. H. Resau, S. A. Courtneidge, The adaptor protein Tks5/Fish is required for podosome formation and function, and for the protease-driven invasion of cancer cells. Cancer Cell 7, 155-165 (2005).
17. P. Lock, C. L. Abram, T. Gibson, S. A. Courtneidge, A new method for isolating tyrosine kinase substrates used to identify fish, an SH3 and PX domain-containing protein, and Src substrate. EMBO J. 17, 4346-4357 (1998).
18. J. D. Lambeth, T. Kawahara, B. Diebold, Regulation of Nox and Duox enzymatic activity and expression. Free Radic. Biol. Med. 43, 319-331 (2007).
19. L. S. Terada, Specificity in reactive oxidant signaling: Think globally, act locally. J. Cell Biol. 174, 615-623 (2006).
20. R. F. Wu, Y. C. Xu, Z. Ma, F. E. Nwariaku, G. A. Sarosi Jr., L. S. Terada, Subcellular targeting of oxidants during endothelial cell migration. J. Cell Biol. 171, 893-904 (2005).
21. N. R. Alexander, K. M. Branch, A. Parekh, E. S. Clark, I. C. Iwueke, S. A. Guelcher, A. M.Weaver, Extracellular matrix rigidity promotes invadopodia activity. Curr. Biol. 18, 1295-1299 (2008).
22. J. Brabek, S. S. Constancio, N. Y. Shin, A. Pozzi, A. M. Weaver, S. K. Hanks, CAS promotes invasiveness of Src-transformed cells. Oncogene 23, 7406-7415 (2004).
23. M. A. Chellaiah, R. S. Biswas, D. Yuen, U. M. Alvarez, K. A. Hruska, Phosphatidylinositol 3,4,5- trisphosphate directs association of Src homology 2-containing signaling proteins with gelsolin. J. Biol. Chem. 276, 47434-47444 (2001).
24. U. Philippar, E. T. Roussos, M. Oser, H. Yamaguchi, H. D. Kim, S. Giampieri, Y. Wang, S. Goswami, J. B. Wyckoff, D. A. Lauffenburger, E. Sahai, J. S. Condeelis, F. B. Gertler, A Mena invasion isoform potentiates EGF-induced carcinoma cell invasion and metastasis. Dev. Cell 15, 813-828 (2008).
25. L. Spinardi, J. Rietdorf, L. Nitsch, M. Bono, C. Tacchetti, M. Way, P. C. Marchisio, A dynamic podosome- like structure of epithelial cells. Exp. Cell Res. 295, 360-374 (2004).
26. The author would like to acknowledge funding from the National Institute of General Medical Sciences (1R01GM075126), National Cancer Institute (1R21DE018244), and American Cancer Society (RSG118085).