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Chuanyue Wu¹ and Shoukat Dedhar^2,3

¹ Department of Pathology, University of Pittsburgh, Pittsburgh, PA 15261
² British Columbia Cancer Agency and The Prostate Center at Vancouver Hospital, Jack Bell Research Center, Vancouver, BC, Canada, V6H3Z6
³ Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, Canada, V6T1Z3

Address correspondence to Shoukat Dedhar, BC Cancer Agency and Jack Bell Research Center, 2660 Oak St. Vancouver, BC, Canada, V6H3Z6. Tel.: (604) 875-5655. Fax: (604) 875-5452. E-mail: sdedhar{at}interchange.ubc.ca

How intracellular cytoskeletal and signaling proteins connect and communicate with the extracellular matrix (ECM) is a fundamental question in cell biology. Recent biochemical, cell biological, and genetic studies have revealed important roles of cytoplasmic integrin-linked kinase (ILK) and its interactive proteins in these processes. Cell adhesion to ECM is an important process that controls cell shape change, migration, proliferation, survival, and differentiation. Upon adhesion to ECM, integrins and a selective group of cytoskeletal and signaling proteins are recruited to cell matrix contact sites where they link the actin cytoskeleton to the ECM and mediate signal transduction between the intracellular and extracellular compartments. In this review, we discuss the molecular activities and cellular functions of ILK, a protein that is emerging as a key component of the cell–ECM adhesion structures.

Key Words: integrins; integrin-linked kinase; cell adhesion; cytoskeleton; signal transduction

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