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Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK.

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Schaller, M D, Borgman, C A, Parsons, J T·1993·Molecular and Cellular Biology

Abstract

Integrins play a central role in cellular adhesion and anchorage of the cytoskeleton and participate in the generation of intracellular signals, including tyrosine phosphorylation. We have recently isolated a cDNA encoding a unique, focal adhesion-associated protein tyrosine kinase (FAK) that is a component of an integrin-mediated signal transduction pathway. Here we report the isolation of cDNAs encoding the C-terminal, noncatalytic domain of the FAK kinase, termed FRNK (FAK-related nonkinase). Both the FAK- and FRNK-encoded polypeptides, pp125FAK and p41/p43FRNK, are expressed in normal chicken embryo cells. pp125FAK and p41/p43FRNK were localized to focal adhesions, suggesting that pp125FAK is directed to the focal adhesions by sequences within its C-terminal domain. We also show that the fibronectin-dependent increase in tyrosine phosphorylation of pp125FAK is accompanied by a concomitant posttranslational modification of p41FRNK.

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Authors
Schaller, M. D., Borgman, C. A., & Parsons, J. T.
Venue
Molecular and Cellular Biology
Published
1993-02
Volume
13
Issue
2
Pages
785-791
ISSN
  • 0270-7306 (ISSN-L)
  • 1098-5549
OpenAlex
W1926397135
Cited by
292
References
0
FWCI
5.98
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK. https://app.cochat.ai/papers/10.1128/mcb.13.2.785
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Schaller, M. D., Borgman, C. A., & Parsons, J. T. (1993). Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.13.2.785

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.