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Biochim Biophys Acta. 2004 Jul 5;1692(2-3):55-62.

The PINCH-ILK-parvin complexes: assembly, functions and regulation.

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  • 1Department of Pathology, University of Pittsburgh, 707B Scaife Hall, 3550 Terrace Street, PA 15261, USA.


Cell-extracellular matrix (ECM) adhesion is mediated by transmembrane cell adhesion receptors (e.g., integrins) and receptor proximal cytoplasmic proteins. Over the past several years, studies using biochemical, structural, cell biological and genetic approaches have provided important evidence suggesting crucial roles of integrin-linked kinase (ILK), PINCH and CH-ILKBP/actopaxin/affixin/parvin (abbreviated as parvin herein) in ECM control of cell behavior. One general theme emerging from these studies is that the formation of ternary protein complexes consisting of ILK, PINCH and parvin is pivotal to the functions of PINCH, ILK and parvin proteins. In addition, recent studies have begun to uncover the molecular mechanisms underlying the assembly, functions and regulation of the PINCH-ILK-parvin (PIP) complexes. The PIP complexes provide crucial physical linkages between integrins and the actin cytoskeleton and transduce diverse signals from ECM to intracellular effectors. Among the challenges of future studies are to define the functions of different PIP complexes in various cellular processes, identify additional partners of the PIP complexes that regulate and/or mediate the functions of the PIP complexes, and determine the roles of the PIP complexes in the pathogenesis of human diseases involving abnormal cell-ECM adhesion and signaling.

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