The integrin-linked kinase regulates cell morphology and motility in a rho-associated kinase-dependent manner.

摘要: The integrin-linked kinase (ILK) is a multidomain focal adhesion protein implicated in signal transmission from integrin and growth factor receptors. We have determined that ILK regulates U2OS osteosarcoma cell spreading motility manner requiring both activity localization. Overexpression of wild-type (WT) resulted suppression spreading, polarization, to fibronectin. Cell lines overexpressing kinase-dead (S343A) or paxillin binding site mutant proteins display inhibited haptotaxis Conversely, was potentiated cells expressing the "dominant negative," non-targeting, kinase-deficient E359K protein. Suppression WT could be rescued by treatment with Rho-associated (ROCK) inhibitor Y-27632 introduction dominant negative ROCK RhoA, suggesting these increased RhoA signaling. Activation (FAK), regulator reduced cells, whereas overexpression FAK observed defects polarity. Thus, ILK-dependent effects on and/or signaling may mediated through FAK.