| First Author | Ciatto C | Year | 2010 |
| Journal | Nat Struct Mol Biol | Volume | 17 |
| Issue | 3 | Pages | 339-47 |
| PubMed ID | 20190755 | Mgi Jnum | J:245329 |
| Mgi Id | MGI:5917803 | Doi | 10.1038/nsmb.1781 |
| Citation | Ciatto C, et al. (2010) T-cadherin structures reveal a novel adhesive binding mechanism. Nat Struct Mol Biol 17(3):339-47 |
| abstractText | Vertebrate genomes encode 19 classical cadherins and about 100 nonclassical cadherins. Adhesion by classical cadherins depends on binding interactions in their N-terminal EC1 domains, which swap N-terminal beta-strands between partner molecules from apposing cells. However, strand-swapping sequence signatures are absent from nonclassical cadherins, raising the question of how these proteins function in adhesion. Here, we show that T-cadherin, a glycosylphosphatidylinositol (GPI)-anchored cadherin, forms dimers through an alternative nonswapped interface near the EC1-EC2 calcium-binding sites. Mutations within this interface ablate the adhesive capacity of T-cadherin. These nonadhesive T-cadherin mutants also lose the ability to regulate neurite outgrowth from T-cadherin-expressing neurons. Our findings reveal the likely molecular architecture of the T-cadherin homophilic interface and its requirement for axon outgrowth regulation. The adhesive binding mode used by T-cadherin may also be used by other nonclassical cadherins. |
