User:Jordan RG Elliott/Sandbox 1

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, truncated cadherins, are a sect of nonclassical cadherin, unique molecules that distinguishes 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 innermembrane or cytoplasmic domain,​ shorteing the total weight, hence the name truncated. (Ranscht B, Dours-Zimmermann MT. T-cadherin, a novel cadherin cell adhesion molecule in the nervous system lacks the conserved cytoplasmic region. Neuron. 1991 Sep;7(3):391-402. doi: 10.1016/0896-6273(91)90291-7. PMID: 1654948.) 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.

Disease

Relevance

Structural highlights

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