Function
The Cadherins are calcium-dependent proteins that mediate cell–cell adhesion and are essential for the development and structural integrity of tissues at the cellular level. Classical cadherins that make up much of the cadherin family, such as E-, N-, and P-cadherins, typically facilitate homophilic adhesion through a mechanism known as “strand swapping,” in which the N-terminal β-strands of cadherin molecules from opposing cells are exchanged. (Gumbiner, B. Regulation of cadherin-mediated adhesion in morphogenesis. Nat Rev Mol Cell Biol 6, 622–634 (2005). https://doi.org/10.1038/nrm1699). Classical cadherins and strand swapping are the standard for many organisms because of their adhesion strength and stability due to their membrane integration and low extra cellular motility.
T-Cadherins, or truncated cadherins, are a subset of nonclassical cadherins, unique molecules that distinguish themselves from the above with different membrane anchorage techniques and functions, while retaining similar motifs and overall structures. The 3K5S T-cadherin is attached peripherally to the cell surface, via a GPI anchor, having no inner membrane or cytoplasmic domain, shortening the total weight, hence the name truncated. (Ciatto, C., Bahna, F., Zampieri, N. et al. T-cadherin structures reveal a novel adhesive binding mechanism. Nat Struct Mol Biol 17, 339–347 (2010). https://doi.org/10.1038/nsmb.1781) This binding method and reduced size is beneficial for 3K5S while acting as a neurite development and signaling aid in chick growth. The increased mobility and lack of rigid structure can allow for a more fluid and less tense growth environment for development.
Structural Highlights
Relevance
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