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A complex of Protocadherin-19 and N-cadherin mediates a novel mechanism of cell adhesion
During embryonic morphogenesis, adhesion molecules are required for selective cell–cell interactions. The classical cadherins mediate homophilic calcium-dependent cell adhesion and are founding members of the large and diverse cadherin superfamily. The protocadherins are the largest subgroup within...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3246890/ https://www.ncbi.nlm.nih.gov/pubmed/22184198 http://dx.doi.org/10.1083/jcb.201108115 |
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author | Emond, Michelle R. Biswas, Sayantanee Blevins, Cheasequah J. Jontes, James D. |
author_facet | Emond, Michelle R. Biswas, Sayantanee Blevins, Cheasequah J. Jontes, James D. |
author_sort | Emond, Michelle R. |
collection | PubMed |
description | During embryonic morphogenesis, adhesion molecules are required for selective cell–cell interactions. The classical cadherins mediate homophilic calcium-dependent cell adhesion and are founding members of the large and diverse cadherin superfamily. The protocadherins are the largest subgroup within this superfamily, yet their participation in calcium-dependent cell adhesion is uncertain. In this paper, we demonstrate a novel mechanism of adhesion, mediated by a complex of Protocadherin-19 (Pcdh19) and N-cadherin (Ncad). Although Pcdh19 alone is only weakly adhesive, the Pcdh19–Ncad complex exhibited robust adhesion in bead aggregation assays, and Pcdh19 appeared to play the dominant role. Adhesion by the Pcdh19–Ncad complex was unaffected by mutations that disrupt Ncad homophilic binding but was inhibited by a mutation in Pcdh19. In addition, the complex exhibited homophilic specificity, as beads coated with Pcdh19–Ncad did not intermix with Ncad- or Pcdh17–Ncad-coated beads. We propose a model in which association of a protocadherin with Ncad acts as a switch, converting between distinct binding specificities. |
format | Online Article Text |
id | pubmed-3246890 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-32468902012-06-26 A complex of Protocadherin-19 and N-cadherin mediates a novel mechanism of cell adhesion Emond, Michelle R. Biswas, Sayantanee Blevins, Cheasequah J. Jontes, James D. J Cell Biol Research Articles During embryonic morphogenesis, adhesion molecules are required for selective cell–cell interactions. The classical cadherins mediate homophilic calcium-dependent cell adhesion and are founding members of the large and diverse cadherin superfamily. The protocadherins are the largest subgroup within this superfamily, yet their participation in calcium-dependent cell adhesion is uncertain. In this paper, we demonstrate a novel mechanism of adhesion, mediated by a complex of Protocadherin-19 (Pcdh19) and N-cadherin (Ncad). Although Pcdh19 alone is only weakly adhesive, the Pcdh19–Ncad complex exhibited robust adhesion in bead aggregation assays, and Pcdh19 appeared to play the dominant role. Adhesion by the Pcdh19–Ncad complex was unaffected by mutations that disrupt Ncad homophilic binding but was inhibited by a mutation in Pcdh19. In addition, the complex exhibited homophilic specificity, as beads coated with Pcdh19–Ncad did not intermix with Ncad- or Pcdh17–Ncad-coated beads. We propose a model in which association of a protocadherin with Ncad acts as a switch, converting between distinct binding specificities. The Rockefeller University Press 2011-12-26 /pmc/articles/PMC3246890/ /pubmed/22184198 http://dx.doi.org/10.1083/jcb.201108115 Text en © 2011 Emond et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Emond, Michelle R. Biswas, Sayantanee Blevins, Cheasequah J. Jontes, James D. A complex of Protocadherin-19 and N-cadherin mediates a novel mechanism of cell adhesion |
title | A complex of Protocadherin-19 and N-cadherin mediates a novel mechanism of cell adhesion |
title_full | A complex of Protocadherin-19 and N-cadherin mediates a novel mechanism of cell adhesion |
title_fullStr | A complex of Protocadherin-19 and N-cadherin mediates a novel mechanism of cell adhesion |
title_full_unstemmed | A complex of Protocadherin-19 and N-cadherin mediates a novel mechanism of cell adhesion |
title_short | A complex of Protocadherin-19 and N-cadherin mediates a novel mechanism of cell adhesion |
title_sort | complex of protocadherin-19 and n-cadherin mediates a novel mechanism of cell adhesion |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3246890/ https://www.ncbi.nlm.nih.gov/pubmed/22184198 http://dx.doi.org/10.1083/jcb.201108115 |
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