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Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin.
Open accessAbstract
A homology-based cDNA cloning approach was used to identify a widely expressed protein-tyrosine kinase designated as "focal adhesion kinase" (FadK). The entire mouse FadK amino acid sequence was deduced from cDNA clones, revealing a large (119-kDa) non-membrane-spanning protein-tyrosine kinase that lacks Src-homology SH2 and SH3 domains. Immunostaining of BALB/c 3T3 fibroblasts revealed that FadK is concentrated in focal adhesions. FadK is phosphorylated on tyrosine in growing cultures of BALB/c 3T3 cells but contains little or no phosphotyrosine in cells detached by trypsinization. The tyrosine-phosphorylated state is regained within minutes when the cells are replated onto fibronectin. Activation of FadK may be an important early step in intracellular signal transduction pathways triggered in response to cell interactions with the extracellular matrix.
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Citations
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“Focal adhesion kinase (FAK) was discovered almost three decades ago as a kinase that is highly phosphorylated in response to cell adhesion and localisation into the focal adhesion complex [1,2].”
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Metadata
- Authors
- Hanks, S. K., Calalb, M. B., Harper, M. C., & Patel, S. K.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1992-09-15
- Volume
- 89
- Issue
- 18
- Pages
- 8487-8491
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2006892275
- Cited by
- 818
- References
- 0
- FWCI
- 14.29
- Type
- journal article
- Language
- en
- Open access
- green
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