Integrin-linked kinase (ILK) and its interactors: a new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes
Cy. Wu et S. Dedhar, Integrin-linked kinase (ILK) and its interactors: a new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes, J CELL BIOL, 155(4), 2001, pp. 505-510
How intracellular cytoskeletal and signaling proteins connect and communica
te with the extracellular matrix (ECM) is a fundamental question in cell bi
ology. Recent biochemical, cell biological, and genetic studies have reveal
ed important roles of cytoplasmic integrin-linked kinase (ILK) and its inte
ractive proteins in these processes. Cell adhesion to ECM is an important p
rocess 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 contac
t sites where they link the actin cytoskeleton to the ECM and mediate signa
l 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 adhesio
n structures.