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Cited by 366

The DOI matches its Crossref record; 134 of the 134 references it cites were found in a registry or an index.

Focal adhesion kinase signaling activities and their implications in the control of cell survival and motility

Open access
Hanks, Steven K·2003·Frontiers in Bioscience
DOI 10.2741/1114
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Abstract

Focal adhesion kinase (FAK) was first described in 1992 as a novel nonreceptor protein-tyrosine kinase localized prominently within focal adhesions, suggesting a signaling role in regulating cell behavior resulting from integrin interaction with the extracellular matrix. Subsequent studies over the past decade have established functional roles for FAK as a positive regulator of both cell motility and cell survival, while providing considerable insight into signaling mechanisms involved. FAK signaling results from its ability to become highly phosphorylated in response to integrin-mediated adhesion on Tyr-397, permitting interactions with a number of different signaling effectors containing Src homology 2 (SH2) domains. Src-family kinases recruited to the Tyr-397 site phosphorylate two FAK-interacting proteins, Crk-associated substrate (CAS) and paxillin, which results ultimately in regulation of Rho-family GTPases contributing to cell motility. CAS phosphorylation, as well as phosphatidylinositol 3-kinase (PI3K) activation resulting from its binding to the FAK Tyr-397 site, have been implicated as downstream FAK signaling events that confer a resistance to apoptosis. This article reviews these and other aspects of FAK signaling and function.

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Metadata

Authors
Hanks, S. K.
Venue
Frontiers in Bioscience
Publisher
IMR Press
Published
2003
Volume
8
Issue
4
Pages
d982-996
ISSN
  • 1093-4715 (ISSN-L)
  • 1093-9946
DOI
10.2741/1114
OpenAlex
W1532590486
Cited by
366
References
134
FWCI
10.66
Type
journal article
Language
en
Open access
bronze

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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).

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