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Nat Commun. 2013;4:1589. doi: 10.1038/ncomms2560.

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

Author information

1
Department of Bioengineering, University of Illinois, Urbana-Champaign, Illinois 61801, USA.

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-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.

PMID:
23481397
PMCID:
PMC3602931
DOI:
10.1038/ncomms2560
[Indexed for MEDLINE]
Free PMC Article

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