Integrin-linked kinase (ILK) and its interactors: a new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes

Authors
Citation
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
Citations number
37
Categorie Soggetti
Cell & Developmental Biology
Journal title
JOURNAL OF CELL BIOLOGY
ISSN journal
00219525 → ACNP
Volume
155
Issue
4
Year of publication
2001
Pages
505 - 510
Database
ISI
SICI code
0021-9525(20011112)155:4<505:IK(AII>2.0.ZU;2-B
Abstract
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.