Migfilin interacts with VASP PathwayStep4794 PathwayStep4797 Formation of the PINCH-ILK-parvin complex MigFilin associates with Filamin and F-actin Mig-2 recruits Migfilin to the cell-ECM adhesions PathwayStep4805 PathwayStep4804 PathwayStep4803 PathwayStep4802 Cell-extracellular matrix interactions Authored: Matthews, L, 2009-10-12 Cell–extracellular matrix (ECM) interactions play a critical role in regulating a variety of cellular processes in multicellular organisms including motility, shape change, survival, proliferation and differentiation. Cell–ECM contact is mediated by transmembrane cell adhesion receptors, such as integrins, that interact with extracellular matrix proteins as well as a number of cytoplasmic adaptor proteins. Many of these adaptor proteins physically interact with the actin cytoskeleton or function in signal transduction. <br>Several protein complexes interact with the cytoplasmic tail of integrins and function in transducing bi-directional signals between the ECM and intracellular signaling pathways (reviewed in Sepulveda et al., 2005).<br>Early events that are triggered by interactions with ECM, such as formation/turnover of Focal Adhesions, regulation of actin dynamics and protrusion of lamellipodia to promote cellular spreading and motility are modulated by PINCH, ILK, parvin complexes (see Sepulveda et al., 2005). A number of partners of the PINCH-ILK-parvin complex components have been identified that regulate and/or mediate the functions of these complexes (reviewed in Wu, 2004). Interactions with some of these partners modulate cytoskeletal remodeling and cell spreading. Edited: Matthews, L, 2009-11-10 Pubmed15246679 Pubmed16314921 Reactome Database ID Release 43446353 Reactome, http://www.reactome.org ReactomeREACT_20649 Reviewed: Wu, C, 2009-11-12 Regulation of cytoskeletal remodeling and cell spreading by IPP complex components Localization of the PINCH-ILK-PARVIN complex to focal adhesions