Cadherin
- Clathrin regulates Wnt/β-catenin signaling by affecting Golgi to plasma membrane transport of transmembrane proteins
Highlighted Article: The exocytic function of clathrin controls the abundance of the Wnt signaling component β-catenin through LRP5/6 and cadherin molecules.
- Scaling up single-cell mechanics to multicellular tissues – the role of the intermediate filament–desmosome network
Summary: A review of the roles of intermediate filaments and desmosomes in mechanobiology, highlighting their integration with other cytoskeletal and adhesive systems.
- Epidermal growth factor receptor and integrins control force-dependent vinculin recruitment to E-cadherin junctions
Summary: E-cadherin force transduction activates a kinase cascade via epidermal growth factor receptor and integrins that regulates force-dependent recruitment of VCL to stressed cadherin adhesions.
- Gα12 is required for renal cystogenesis induced by Pkd1 inactivation
Summary: Deletion of the gene encoding the G-protein subunit Gα12 prevents mouse kidneys from developing the kidney cysts induced by Pkd1 inactivation, which indicates that Gα12 signaling is crucial for renal cystogenesis.
- Divergence of structural strategies for homophilic E-cadherin binding among bilaterians
Summary: Atomic force microscopy imaging revealed that Drosophila E-cadherin has a tightly folded globular structure with multiple domains that contain determinants of homophilic binding.
- Molecular organization of the desmosome as revealed by direct stochastic optical reconstruction microscopy
Highlighted Article: The nanoscale organization of proteins in the desmosome, a structure mediating strong cell–cell adhesion, is elucidated by dSTORM super-resolution fluorescence microscopy.
- p120-catenin controls contractility along the vertical axis of epithelial lateral membranes
Highlighted Article: The distinct activities of p120 towards E-cadherin and Rho are molecularly and functionally coupled, and this in turn enables the maintenance of cell shape in the larger context of an epithelial monolayer.