The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
Inhibition of Cell Spreading by Expression of the C-Terminal Domain of Focal Adhesion Kinase (FAK) Is Rescued by Coexpression of Src or Catalytically Inactive FAK: a Role for Paxillin Tyrosine Phosphorylation
Open accessAbstract
pp125FAK is a tyrosine kinase that appears to regulate the assembly of focal adhesions and thereby promotes cell spreading on the extracellular matrix. In some cells, the C terminus of pp125FAK is expressed as a separate protein, pp41/43FRNK. We have previously shown that overexpression of pp41/43FRNK inhibits tyrosine phosphorylation of pp125FAK and paxillin and, in addition, delays cell spreading and focal adhesion assembly. Thus, pp41/43FRNK functions as a negative inhibitor of adhesion signaling and provides a tool to dissect the mechanism by which pp125FAK promotes cell spreading. We report here that the inhibitory effects of pp41/43FRNK expression can be rescued by the co-overexpression of wild-type pp125FAK and partially rescued by catalytically inactive variants of pp125FAK. However, coexpression of an autophosphorylation site mutant of pp125FAK, which fails to bind the SH2 domain of pp60c-Src, or a mutant that fails to bind paxillin did not promote cell spreading. In contrast, expression of pp41/43FRNK and pp60c-Src reconstituted cell spreading and tyrosine phosphorylation of paxillin but did so without inducing tyrosine phosphorylation of pp125FAK. These data provide additional support for a model whereby pp125FAK acts as a "switchable adaptor" that recruits pp60c-Src to phosphorylate paxillin, promoting cell spreading. In addition, these data point to tyrosine phosphorylation of paxillin as being a critical step in focal adhesion assembly.
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Cites
Integrins: Versatility, modulation, and signaling in cell adhesion
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Cell Migration: A Physically Integrated Molecular Process
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Focal Adhesions: Transmembrane Junctions Between the Extracellular Matrix and the Cytoskeleton
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FOCAL ADHESIONS, CONTRACTILITY, AND SIGNALING
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Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice
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Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
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Actin-Based Cell Motility and Cell Locomotion
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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
Self-citationIntegrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness
Palecek, S. P., Loftus, J. C., Ginsberg, M. H., Lauffenburger, D. A., & Horwitz, A. F. (1997) · Nature · doi:10.1038/385537a0 · Cited by 1,427
Cited by
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
Laukaitis, C. M., Webb, D. J., Donais, K., & Horwitz, A. F. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.7.1427 · Cited by 455
Focal adhesion kinase in integrin-mediated signaling
Cary, L. (1999) · Frontiers in Bioscience · doi:10.2741/cary · Cited by 346
Sieg, D. J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.20.5933 · Cited by 339
Han, H.-Y., Zhang, J.-P., Ji, S.-Q., Liang, Q.-M., Kang, H.-C., Tang, R.-H., Zhu, S.-Q., & Xue, Z. (2013) · PLoS ONE · doi:10.1371/journal.pone.0064839 · Cited by 20
Metadata
- Authors
- Richardson, A., Malik, R. K., Hildebrand, J. D., & Parsons, J. T.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 1997-12-01
- Volume
- 17
- Issue
- 12
- Pages
- 6906-6914
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2120346794
- Cited by
- 331
- References
- 51
- FWCI
- 10.81
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Inhibition of Cell Spreading by Expression of the C-Terminal Domain of Focal Adhesion Kinase (FAK) Is Rescued by Coexpression of Src or Catalytically Inactive FAK: a Role for Paxillin Tyrosine Phosphorylation. https://app.cochat.ai/papers/10.1128/mcb.17.12.6906
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- Richardson, A., Malik, R. K., Hildebrand, J. D., & Parsons, J. T. (1997). Inhibition of Cell Spreading by Expression of the C-Terminal Domain of Focal Adhesion Kinase (FAK) Is Rescued by Coexpression of Src or Catalytically Inactive FAK: a Role for Paxillin Tyrosine Phosphorylation. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.17.12.6906
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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