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Focal adhesion kinase in integrin-mediated signaling

L A Cary1, J L Guan

  • 1Department of Molecular Medicine, Cornell University, Ithaca, NY 14853, USA.

Frontiers in Bioscience : a Journal and Virtual Library
|January 16, 1999
PubMed

Insights

Integrins signal through focal adhesion kinase (FAK) to control cell behavior. This review details FAK

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Integrins are cell surface receptors that bind extracellular matrix proteins.
  • Integrin engagement initiates intracellular signaling pathways.
  • These pathways regulate critical cellular functions like migration, proliferation, and apoptosis.

Purpose of the Study:

  • To discuss the mechanisms of integrin-mediated activation and localization of focal adhesion kinase (FAK).
  • To present the interactions between FAK and other signaling/cytoskeletal proteins.
  • To highlight FAK's role in regulating integrin-mediated cellular processes.

Main Methods:

  • Literature review of studies on integrin signaling and FAK.
  • Analysis of protein-protein interactions involving FAK.
  • Discussion of FAK's functional outcomes in cellular events.

Main Results:

  • Integrin signaling activates FAK, a key protein tyrosine kinase.
  • FAK interacts with proteins such as Src, PI3K, Grb2, p130Cas, and paxillin.
  • These interactions mediate FAK's downstream effects on cell behavior.

Conclusions:

  • FAK is central to integrin signaling, linking cell adhesion to intracellular events.
  • FAK promotes cell migration, proliferation, and spreading.
  • FAK plays a role in preventing programmed cell death (apoptosis).

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