Histol Histopathol, Vol 17, Abbi and Guan (original) (raw)

Review

Focal adhesion kinase: Protein interactions and cellular functions

S. Abbi and J.L. Guan

Department of Molecular Medicine, Cornell University, Ithaca, NY, USA

Offprint requests to: Jun-Lin Guan, Department of Molecular Medicine, Cornell University, Ithaca, NY 14853, USA, Fax: (607) 253-3708. e-mail: jg19@cornell.edu

Summary. Integrin-mediated cell adhesion to extracellular matrix (ECM) plays important roles in a variety of biological processes. Recent studies suggested that integrins mediate signal transduction across the plasma membrane via activating several intracellular signaling pathways. Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase that has been shown to be a major mediator of integrin signal transduction pathways. Upon activation by integrins, FAK undergoes autophosphorylation as well as associations with several other intracellular signaling molecules. These interactions in the signaling pathways have been shown to regulation a variety of cellular functions such as cell spreading, migration, cell proliferation, apoptosis and cell survival. Recent progress in the understanding of FAK interactions with other proteins in the regulation of these cellular functions will be discussed in this review. Histol. Histopathol. 17, 1163-1171 (2002)

Key words: Extracellular matrix (ECM), Integrins, Focal adhesion kinase (FAK), Signal transduction

DOI: 10.14670/HH-17.1163