More Like this

1. Epidermal melanocytes in segmental vitiligo show altered expression of E‐cadherin, but not P‐cadherin

   https://doi.org/10.1111/bjd.16352  

   Grill, C. ; Benzekri, L. ; Rubod, A. ; Aktary, Z. ; Ezzedine, K. ; Taïeb, A. ; Gauthier, Y. ; Larue, L. ; Delmas, V. ( March 2018 , British Journal of Dermatology)
2. Push-pull mechanics of E-cadherin ectodomains

   K. Nagendra, A. Izzet ( April 2023 , Biophysical journal)

   E-cadherin plays a central role in cell-cell adhesion. The ectodomains of wild type cadherins form a crystalline- like two dimensional lattice in cell-cell interfaces mediated by both trans (apposed cell) and cis (same cell) interactions. In addition to these extracellular forces, adhesive strength is further regulated by cytosolic phenomena involving 𝛼 and 𝛽- catenin–mediated interactions between cadherin and the actin cytoskeleton. Cell-cell adhesion can be further strengthened under tension through mechanisms that have not been definitively characterized in molecular detail. Here we quantitatively determine the role of the cadherin ectodomain in mechanosensing. To this end, we devise an E-cadherin-coated emulsion system, in which droplet surface tension is balanced by protein binding strength to give rise to stable areas of adhesion. To reach the honeycomb/cohesive limit, an initial emulsion compression by centrifugation facilitates E-cadherin trans-binding, while a high protein surface concentration enables the cis-enhanced stabilization of the interface. We observe an abrupt concentration dependence on recruitment into adhesions of constant crystalline density, reminiscent of a first-order phase transition. Removing the lateral cis-interaction with a "cis mutant" shifts this transition to higher surface densities leading to denser, yet weaker adhesions. In both proteins, the stabilization of progressively larger areas of deformation can be rationalized by a stiffening catch-bond, whose strength increases with tension. This catch bond may well correspond to one that has been identified in the cadherin “X-dimer". 

   more » « less
3. Cadherin genes and evolutionary novelties in the octopus

   https://doi.org/10.1016/j.semcdb.2017.06.007  

   Wang, Z. Yan ; Ragsdale, Clifton W. ( September 2017 , Seminars in Cell & Developmental Biology)
4. Computational model of E-cadherin clustering under force

   https://doi.org/10.1016/j.bpj.2021.10.018  

   Chen, Yang ; Brasch, Julia ; Harrison, Oliver J. ; Bidone, Tamara C. ( November 2021 , Biophysical Journal)
5. Mapping transmembrane binding partners for E-cadherin ectodomains

   https://doi.org/10.1073/pnas.2010209117  

   Shafraz, Omer ; Xie, Bin ; Yamada, Soichiro ; Sivasankar, Sanjeevi ( November 2020 , Proceedings of the National Academy of Sciences)

   We combine proximity labeling and single molecule binding assays to discover transmembrane protein interactions in cells. We first screen for candidate binding partners by tagging the extracellular and cytoplasmic regions of a “bait” protein with BioID biotin ligase and identify proximal proteins that are biotin tagged on both their extracellular and intracellular regions. We then test direct binding interactions between proximal proteins and the bait, using single molecule atomic force microscope binding assays. Using this approach, we identify binding partners for the extracellular region of E-cadherin, an essential cell–cell adhesion protein. We show that the desmosomal proteins desmoglein-2 and desmocollin-3, the focal adhesion protein integrin-α2β1, the receptor tyrosine kinase ligand ephrin-B1, and the classical cadherin P-cadherin, all directly interact with E-cadherin ectodomains. Our data shows that combining extracellular and cytoplasmic proximal tagging with a biophysical binding assay increases the precision with which transmembrane ectodomain interactors can be identified.

    

   more » « less