The DOI matches its Crossref record; 70 of the 70 references it cites were found in a registry or an index.
Signaling through focal adhesion kinase
Abstract
Focal adhesion kinase (FAK) is a nonreceptor protein‐tyrosine kinase implicated in controlling cellular responses to the engagement of cell‐surface integrins, including cell spreading and migration, survival and proliferation. Aberrant FAK signaling may contribute to the process of cell transformation by certain oncoproteins, including v‐Src. Progress toward elucidating the events leading to FAK activation following integrin‐mediated cell adhesion, as well as events downstream of FAK, has come through the identification of FAK phosphorylation sites and interacting proteins. A signaling partnership is formed between FAK and Src‐family kinases, leading to tyrosine phosphorylation of FAK and associated ‘docking’ proteins Cas and paxillin. Subsequent recruitment of proteins containing Src homology 2 domains, including Grb2 and c‐Crk, to the complex is likely to trigger adhesion‐induced cellular responses, including changes to the actin cytoskeleton and activation of the Ras‐MAP kinase pathway.
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Cites
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Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice
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Rho-stimulated contractility drives the formation of stress fibers and focal adhesions.
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Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
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Self-citationIntegrins: Emerging Paradigms of Signal Transduction
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pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions.
Schaller, M. D., Borgman, C. A., Cobb, B. S., Vines, R. R., Reynolds, A. B., & Parsons, J. T. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.11.5192 · Cited by 1,444
Regulation, substrates and functions of src
Brown, M. T., & Cooper, J. A. (1996) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/0304-419x(96)00003-0 · Cited by 1,172
Autophosphorylation of the Focal Adhesion Kinase, ppl25FAK, Directs SH2-Dependent Binding of pp60src
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Control of adhesion-dependent cell survival by focal adhesion kinase.
Frisch, S. M., Vuori, K., Ruoslahti, E., & Chan-Hui, P. Y. (1996) · The Journal of cell biology · doi:10.1083/jcb.134.3.793 · Cited by 1,109
Crystal structure of the tyrosine kinase domain of the human insulin receptor
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Cited by
Calcium's Role in Mechanotransduction during Muscle Development
Benavides Damm, T., & Egli, M. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000356667 · Cited by 14,502
Mammalian Caspases: Structure, Activation, Substrates, and Functions During Apoptosis
Earnshaw, W. C., Martins, L. M., & Kaufmann, S. H. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.383 · Cited by 2,760
Src family kinases are required for integrin but not PDGFR signal transduction
Klinghoffer, R. A., Sachsenmaier, C., Cooper, J. A., & Soriano, P. (1999) · The EMBO Journal · doi:10.1093/emboj/18.9.2459 · Cited by 731
Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration
Sieg, D. J., Hauck, C. R., & Schlaepfer, D. D. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.16.2677 · Cited by 687
CAS/Crk Coupling Serves as a “Molecular Switch” for Induction of Cell Migration
Klemke, R. L., Leng, J., Molander, R., Brooks, P. C., Vuori, K., & Cheresh, D. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.4.961 · Cited by 659
Metadata
- Authors
- Hanks, S. K., & Polte, T. R.
- Venue
- BioEssays
- Publisher
- Wiley
- Published
- 1997-02
- Volume
- 19
- Issue
- 2
- Pages
- 137-145
- ISSN
- 0265-9247 (ISSN-L)
- 1521-1878
- OpenAlex
- W2160839395
- Cited by
- 469
- References
- 70
- FWCI
- 3.44
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
