The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK.
Open accessAbstract
Focal adhesion kinase (pp125FAK) is localized to focal adhesions and tyrosine phosphorylated by the engagement of beta 1 integrins. However, it is unclear how pp125FAK is linked to integrin molecules. We demonstrate that pp125FAK is directly associated with paxillin, a 68-kD cytoskeleton protein. The COOH-terminal domain of pp125FAK spanning FAK residues 919-1042 is sufficient for paxillin binding and has vinculin-homologous amino acids, which are essential for paxillin binding. Microinjection and subsequent immunohistochemical analysis reveal that glutathione S-transferase-FAK fusion proteins, which bind to paxillin, localize to focal adhesions, whereas fusion proteins with no paxillin-binding activity do not localize to focal adhesions. These findings strongly suggest that pp125FAK is localized to focal adhesions by the direct association with paxillin.
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Cites
Calcium's Role in Mechanotransduction during Muscle Development
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Focal Adhesions: Transmembrane Junctions Between the Extracellular Matrix and the Cytoskeleton
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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
VLA Proteins In The Integrin Family: Structures, Functions, And Their Role On Leukocytes
Hemler, M. (1990) · Annual Review of Immunology · doi:10.1146/annurev.immunol.8.1.365 · Cited by 1,567
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
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Autophosphorylation of the Focal Adhesion Kinase, ppl25FAK, Directs SH2-Dependent Binding of pp60src
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Cited by
Intracellular Delivery by Membrane Disruption: Mechanisms, Strategies, and Concepts
Stewart, M. P., Langer, R., & Jensen, K. F. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00678 · Cited by 747
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
Ilić, D., Almeida, E. A. C., Schlaepfer, D. D., Dazin, P., Aizawa, S., & Damsky, C. H. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.2.547 · Cited by 495
Signaling through focal adhesion kinase
Hanks, S. K., & Polte, T. R. (1997) · BioEssays · doi:10.1002/bies.950190208 · Cited by 469
FAK signaling in human cancer as a target for therapeutics
Lee, B. Y., Timpson, P., Horvath, L. G., & Daly, R. J. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.10.001 · Cited by 425
Metadata
- Authors
- Tachibana, K., Sato, T., D'Avirro, N., & Morimoto, C.
- Venue
- The Journal of experimental medicine
- Publisher
- Rockefeller University Press
- Published
- 1995-10-01
- Volume
- 182
- Issue
- 4
- Pages
- 1089-1099
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- OpenAlex
- W2081135891
- Cited by
- 255
- References
- 40
- FWCI
- 6.23
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK. https://app.cochat.ai/papers/10.1084/jem.182.4.1089
- The paper
- Tachibana, K., Sato, T., D'Avirro, N., & Morimoto, C. (1995). Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK. The Journal of experimental medicine. https://doi.org/10.1084/jem.182.4.1089
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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.
