A complex of Protocadherin-19 and N-cadherin mediates a novel mechanism of cell adhesion
- Authors
- Emond, M.R., Biswas, S., Blevins, C.J., and Jontes, J.D.
- ID
- ZDB-PUB-120727-32
- Date
- 2011
- Source
- The Journal of cell biology 195(7): 1115-1121 (Journal)
- Registered Authors
- Emond, Michelle, Jontes, James
- Keywords
- none
- MeSH Terms
-
- Animals
- CHO Cells
- Cadherins/metabolism*
- Cell Adhesion
- Cell Aggregation
- Cricetinae
- HEK293 Cells
- Humans
- Multiprotein Complexes
- Zebrafish
- Zebrafish Proteins/metabolism*
- PubMed
- 22184198 Full text @ J. Cell Biol.
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.