Journal of Cell Science, Vol 103, Issue 4 943-951, Copyright © 1992 by Company of Biologists

JOURNAL ARTICLES

A chimeric N-cadherin/beta 1-integrin receptor which localizes to both cell-cell and cell-matrix adhesions

B Geiger, D Salomon, M Takeichi and RO Hynes
Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.

To study the molecular mechanisms involved in formation of cell contacts, we have transfected cultured cells with a chimeric cDNA encoding the cytoplasmic and transmembrane domains of beta 1 integrin and the extracellular region of N-cadherin and determined the subcellular distribution of the chimeric molecule. We show that the chimeric receptor associates preferentially with cell-matrix focal contacts, suggesting that its distribution is directed by its beta 1 integrin segment, presumably via interactions of the cytoplasmic domain with cytoskeletal elements characteristic of focal contacts. Transfected cells which expressed relatively high levels of the cadherin/integrin chimera underwent an apparent epithelialization and contained the molecule both in cell-matrix and cell-cell contacts. Location in cell-cell contacts indicates competence of the cadherin extracellular domain to participate in formation of cell-cell junctions using a foreign cytoplasmic domain. Labeling of these cultures for talin, which is normally associated only with matrix adhesions, revealed specific labeling along the newly formed intercellular junctions. This suggests that the local association of talin with these sites is induced by the cytoplasmic tail of beta 1 integrin receptor presented by the chimeric protein. These results suggest that the formation of adherens-type junctions is driven by the cooperative interactions of the relevant adhesion molecules (cadherins and integrins) both with the respective extracellular ligands and with the cytoskeleton.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

				D. B. Alexander, H. Ichikawa, J. F. Bechberger, V. Valiunas, M. Ohki, C. C. G. Naus, T. Kunimoto, H. Tsuda, W. T. Miller, and G. S. Goldberg Normal Cells Control the Growth of Neighboring Transformed Cells Independent of Gap Junctional Communication and Src Activity Cancer Res., February 15, 2004; 64(4): 1347 - 1358. [Abstract] [Full Text] [PDF]

				A. Mastrangelo, S. Homan, M. Humphries, and S. LaFlamme Amino acid motifs required for isolated beta cytoplasmic domains to regulate 'in trans' beta1 integrin conformation and function in cell attachment J. Cell Sci., January 1, 1999; 112(2): 217 - 229. [Abstract] [PDF]

				H. Priddle, L. Hemmings, S. Monkley, A. Woods, B. Patel, D. Sutton, G. A. Dunn, D. Zicha, and D. R. Critchley Disruption of the Talin Gene Compromises Focal Adhesion Assembly in Undifferentiated but Not Differentiated Embryonic Stem Cells J. Cell Biol., August 24, 1998; 142(4): 1121 - 1133. [Abstract] [Full Text] [PDF]

				X Li, M. Graner, E. Williams, C. Roote, T. Bunch, and S Zusman Requirements for the cytoplasmic domain of the alphaPS1, alphaPS2 and betaPS integrin subunits during Drosophila development Development, January 2, 1998; 125(4): 701 - 711. [Abstract] [PDF]

				D Hanein, B Geiger, and L Addadi Differential adhesion of cells to enantiomorphous crystal surfaces Science, March 11, 1994; 263(5152): 1413 - 1416. [Abstract] [PDF]

				A. Meijne, D. Casey, C. Feltkamp, and E Roos Immuno-EM localization of the beta 1 integrin subunit in wet-cleaved fibronectin-adherent fibroblasts J. Cell Sci., January 5, 1994; 107(5): 1229 - 1239. [Abstract] [PDF]