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

Ouyang M, Lu S, Kim T, Chen CE, Seong J, Leckband DE, Wang F, Reynolds AB, Schwartz MA, Wang Y
Nat Commun. 2013 4: 1589

PMID: 23481397 · PMCID: PMC3602931 · DOI:10.1038/ncomms2560

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-p120 catenin 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-p120 catenin 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.

MeSH Terms (23)

Actin Cytoskeleton Animals beta Catenin Cadherins Catenins Cell Polarity Chickens CHO Cells Cricetinae Embryo, Mammalian Fibroblasts Fluorescent Dyes Integrins Intercellular Junctions Mice Models, Biological Phosphatidylinositol 3-Kinases Protein Binding rac GTP-Binding Proteins Rats Recombinant Fusion Proteins RNA, Small Interfering Signal Transduction

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