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N-cadherin regulates spatially polarized signals through distinct p120ctn and β-catenin-dependent signalling pathways

Author

Listed:
  • Mingxing Ouyang

    (University of Illinois
    Beckman Institute for Advanced Science and Technology, University of Illinois
    School of Medicine, Yale University)

  • Shaoying Lu

    (University of Illinois
    Beckman Institute for Advanced Science and Technology, University of Illinois)

  • Taejin Kim

    (Beckman Institute for Advanced Science and Technology, University of Illinois
    Neuroscience Program, University of Illinois)

  • Chin-En Chen

    (Beckman Institute for Advanced Science and Technology, University of Illinois)

  • Jihye Seong

    (Beckman Institute for Advanced Science and Technology, University of Illinois
    Neuroscience Program, University of Illinois)

  • Deborah E. Leckband

    (University of Illinois)

  • Fei Wang

    (University of Illinois)

  • Albert B. Reynolds

    (Vanderbilt University School of Medicine)

  • Martin A. Schwartz

    (School of Medicine, Yale University
    University of Virginia)

  • Yingxiao Wang

    (University of Illinois
    Beckman Institute for Advanced Science and Technology, University of Illinois
    Neuroscience Program, University of Illinois
    Center for Biophysics and Computational Biology, and Institute of Genomic Biology, University of Illinois)

Abstract

The spatial distribution of molecular signals within cells is crucial for cellular functions. Here, as a model to study the polarized spatial distribution of molecular activities, we used cells on micropatterned strips of fibronectin with one end free and the other end contacting a neighbouring cell. Phosphoinositide 3-kinase and the small GTPase Rac display greater activity at the free end, whereas myosin II light chain and actin filaments are enriched near the intercellular junction. Phosphoinositide 3-kinase and Rac polarization depend specifically on the N-cadherin–p120catenin complex, whereas myosin II light chain and actin filament polarization depend on the N-cadherin–β-catenin complex. Integrins promote high phosphoinositide 3-kinase/Rac activities at the free end, and the N-cadherin–p120catenin complex excludes integrin α5 at the junctions to suppress local phosphoinositide 3-kinase and Rac activity. We hence conclude that N-cadherin couples with distinct effectors to polarize phosphoinositide 3-kinase/Rac and myosin II light chain/actin filaments in migrating cells.

Suggested Citation

  • Mingxing Ouyang & Shaoying Lu & Taejin Kim & Chin-En Chen & Jihye Seong & Deborah E. Leckband & Fei Wang & Albert B. Reynolds & Martin A. Schwartz & Yingxiao Wang, 2013. "N-cadherin regulates spatially polarized signals through distinct p120ctn and β-catenin-dependent signalling pathways," Nature Communications, Nature, vol. 4(1), pages 1-12, June.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms2560
    DOI: 10.1038/ncomms2560
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