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SH2- and SH3-mediated Interactions between Focal Adhesion Kinase and Src
Open accessAbstract
Intramolecular SH2 and SH3 interactions mediate enzymatic repression of the Src kinases. One mechanism of activation is disruption of these interactions by the formation of higher affinity SH2 and SH3 interactions with specific ligands. We show that a consensus Src SH3-binding site residing upstream of the Src SH2-binding site in FAK can function as a ligand for the Src SH3 domain. Surface plasmon resonance experiments indicate that a FAK peptide containing both the Src SH2- and SH3-binding sites exhibits increased affinity for Src. Furthermore, the presence of both sites in vitro more potently activates c-Src. A FAK mutant (FAKPro-2) with substitutions destroying the SH3-binding site shows reduced binding to Src in vivo. This mutation also reduces Src-dependent tyrosine phosphorylation on the mutant itself and downstream substrates, such as paxillin. These observations suggest that an SH3-mediated interaction between Src-like kinases and FAK may be important for complex formation and downstream signaling in vivo.
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Cites
Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
Schlaepfer, D. D., Hanks, S. K., Hunter, T., & Geer, P. V. D. (1994) · Nature · doi:10.1038/372786a0 · Cited by 1,595
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Polacheck, W. J., Charest, J. L., & Kamm, R. D. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103581108 · Cited by 509
Mechanisms that regulate adaptor binding to β-integrin cytoplasmic tails
Legate, K. R., & Fässler, R. (2009) · Journal of Cell Science · doi:10.1242/jcs.041624 · Cited by 370
The modular logic of signaling proteins: building allosteric switches from simple binding domains
Lim, W. A. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00290-7 · Cited by 151
Villa-Diaz, L. G., Kim, J. K., Laperle, A., Palecek, S. P., & Krebsbach, P. H. (2016) · Stem Cells · doi:10.1002/stem.2349 · Cited by 77
Dilly, A. K., & Rajala, R. V. S. (2008) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.08-2286 · Cited by 48
Specific interactions of neuronal focal adhesion kinase isoforms with Src kinases and amphiphysin
Messina, S., Onofri, F., Bongiorno‐Borbone, L., Giovedì, S., Valtorta, F., Girault, J., & Benfenati, F. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01519.x · Cited by 26
SRC at the Crossroads of KRAS Inhibitor Resistance: Mechanisms and Therapeutic Opportunities
Tian, H., Zhao, D., Zhou, Z., Kim, A., Huang, H., Lee, Y. J., Qu, Z., Kang, R., Zeh, H. J., Westover, K. D., et al. (2026) · Cancer Letters · doi:10.1016/j.canlet.2025.218194 · Cited by 7
Molecularly imprinted nanoparticles reveal regulatory scaffolding features in Pyk2 tyrosine kinase
Zanela, T. M. P., Zangiabadi, M., Zhao, Y., & Underbakke, E. S. (2024) · RSC Chemical Biology · doi:10.1039/d3cb00228d · Cited by 3
Metadata
- Authors
- Thomas, J. W., Ellis, B., Boerner, R. J., Knight, W. B., White, G. C., & Schaller, M. D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1998-01
- Volume
- 273
- Issue
- 1
- Pages
- 577-583
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2043761739
- Cited by
- 254
- References
- 1
- FWCI
- 5.97
- Type
- journal article
- Language
- en
- Open access
- hybrid
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