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Regulation of Adhesion and Migration by the Rsu1- and PINCH1-mediated Inhibition of Focal Adhesion Formation and Actin Polymerization

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Technical Report

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Uniformed Services University of the Health Sciences Bethesda United States

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The Rsu1-ILK-PINCH-Parvin RIPP complex functions as an adaptor between integrins and the actin cytoskeleton and contributes to the regulation of adhesion and migration. The IPP focal adhesion FA complex is composed of the proteins ILK, PINCH1 and Parvin as well as an associated protein Rsu1, which binds to the LIM 5 domain of the adaptor protein PINCH1. Depletion of Rsu1 or PINCH1 inhibits mammary epithelial cell adhesion and migration. While Rsu1 binding to PINCH1 and the complex is associated with processes such as cell adhesion and migration, the exact mechanism by which this occurs remains to be elucidated. The present work investigates the mechanistic role of Rsu1 in IPP signaling. Our data demonstrated the effects of Rsu1 and PINCH1 depletion on adhesion, migration, FA formation and actin cytoarchitecture in MCF-10A cells. truncated

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