p120-catenin binding masks an endocytic signal conserved in classical cadherins

@article{Nanes2012p120cateninBM,
  title={p120-catenin binding masks an endocytic signal conserved in classical cadherins},
  author={B. Nanes and Christine Chiasson-MacKenzie and Anthony M. Lowery and N. Ishiyama and V. Faundez and M. Ikura and P. Vincent and A. Kowalczyk},
  journal={The Journal of Cell Biology},
  year={2012},
  volume={199},
  pages={365 - 380}
}
p120 regulates adhesive junction dynamics through binding to a dual-function motif in classical cadherins that alternately serves as a p120-binding interface and an endocytic signal. 
Regulation of endothelial barrier function by p120-catenin∙VE-cadherin interaction
The VE-cadherin cytoplasmic domain undergoes proteolytic processing during endocytosis
p120-catenin and β-catenin differentially regulate cadherin adhesive function
Two tyrosine-based sorting signals in the Cx43 C-terminus cooperate to mediate gap junction endocytosis
p120-catenin regulates VE-cadherin endocytosis and degradation induced by the Kaposi sarcoma–associated ubiquitin ligase K5
E-cadherin phosphorylation occurs during its biosynthesis to promote its cell surface stability and adhesion
Dynamic microtubules produce an asymmetric E-cadherin–Bazooka complex to maintain segment boundaries
Protein exchange is reduced in calcium-independent epithelial junctions
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Selective Uncoupling of P120ctn from E-Cadherin Disrupts Strong Adhesion
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Drosophila p120catenin plays a supporting role in cell adhesion but is not an essential adherens junction component
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