Coupling Assembly of the E-Cadherin/β-Catenin Complex to Efficient Endoplasmic Reticulum Exit and Basal-lateral Membrane Targeting of E-Cadherin in Polarized MDCK Cells

@article{Chen1999CouplingAO,
  title={Coupling Assembly of the E-Cadherin/β-Catenin Complex to Efficient Endoplasmic Reticulum Exit and Basal-lateral Membrane Targeting of E-Cadherin in Polarized MDCK Cells },
  author={Y T Chen and Daniel B. Stewart and W. James Nelson},
  journal={The Journal of Cell Biology},
  year={1999},
  volume={144},
  pages={687 - 699}
}
The E-cadherin/catenin complex regulates Ca++-dependent cell-cell adhesion and is localized to the basal-lateral membrane of polarized epithelial cells. Little is known about mechanisms of complex assembly or intracellular trafficking, or how these processes might ultimately regulate adhesion functions of the complex at the cell surface. The cytoplasmic domain of E-cadherin contains two putative basal-lateral sorting motifs, which are homologous to sorting signals in the low density lipoprotein… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 129 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 57 references

Isolation of the cDNA encoding glycoprotein - 2 ( GP2 ) , the major zymogen granule membrane protein . Homology to uromodulin / Tamm - Horsfall protein

  • A. H. Huber, W. J. Nelson, W. I. Weis
  • J . Biol . Chem .
  • 1997
Highly Influential
2 Excerpts

Similar Papers

Loading similar papers…