Title |
An RPTPα/Src family kinase/Rap1 signaling module recruits myosin IIB to support contractile tension at apical E-cadherin junctions
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Published in |
Molecular Biology of the Cell, January 2015
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DOI | 10.1091/mbc.e14-07-1223 |
Pubmed ID | |
Authors |
Guillermo A. Gomez, Robert W. McLachlan, Selwin K. Wu, Benjamin J. Caldwell, Elliott Moussa, Suzie Verma, Michele Bastiani, Rashmi Priya, Robert G. Parton, Katharina Gaus, Jan Sap, Alpha S. Yap |
Abstract |
Cell-cell adhesion couples the contractile cortices of epithelial cells together, generating tension to support a range of morphogenetic processes. E-cadherin adhesion plays an active role in generating junctional tension, by promoting actin assembly and cortical signaling pathways that regulate Myosin II. Multiple Myosin II paralogs accumulate at mammalian epithelial cell-cell junctions. Earlier we found that Myosin IIA responds to Rho-ROCK signaling to support junctional tension in MCF-7 cells. Although Myosin IIB is also found at the zonula adherens (ZA) in these cells, its role in junctional contractility, and its mode of regulation, are less well understood. We now demonstrate that Myosin IIB contributes to tension at the epithelial ZA. Further, we identify a RPTPα-SFK-Rap1 pathway as responsible for recruiting Myosin IIB to the ZA and supporting contractile tension. Overall, these findings reinforce the concept that orthogonal E-cadherin-based signaling pathways recruit distinct Myosin II paralogs to generate the contractile apparatus at apical epithelial junctions. |
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