N-cadherin regulates spatially polarized signals through distinct p120ctn and β-catenin-dependent signalling pathways
Mingxing Ouyang,
Shaoying Lu,
Taejin Kim,
Chin-En Chen,
Jihye Seong,
Deborah E. Leckband,
Fei Wang,
Albert B. Reynolds,
Martin A. Schwartz () and
Yingxiao Wang ()
Additional contact information
Mingxing Ouyang: University of Illinois
Shaoying Lu: University of Illinois
Taejin Kim: Beckman Institute for Advanced Science and Technology, 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
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
Yingxiao Wang: University of Illinois
Nature Communications, 2013, vol. 4, issue 1, 1-12
Abstract:
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.
Date: 2013
References: Add references at CitEc
Citations:
Downloads: (external link)
https://www.nature.com/articles/ncomms2560 Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms2560
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/ncomms2560
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().