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

Abstract

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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Document Details

Document Type
Technical Report
Publication Date
Jun 08, 2012
Accession Number
AD1013096

Entities

People

  • Reyda P. Gonzalez-nieves

Organizations

  • Uniformed Services University of the Health Sciences

Tags

DTIC Thesaurus Topics

  • Biomedical And Dental Materials
  • Breast Cancer
  • Cell Membrane
  • Cell Membrane Structures
  • Cell Movement
  • Cell Physiological Processes
  • Cells
  • Chemical Synthesis
  • Chemistry
  • Cytoskeleton
  • Molecular Biology
  • Neoplasms
  • Polymer Chemistry
  • Polymeric Films
  • Proteins

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