A PDZ-binding motif controls basolateral targeting of syndecan-1 along the biosynthetic pathway in polarized epithelial cells.

@article{Maday2008APM,
  title={A PDZ-binding motif controls basolateral targeting of syndecan-1 along the biosynthetic pathway in polarized epithelial cells.},
  author={Sandra Maday and Eric Michael Anderson and Henry C. Chang and James Shorter and Ayano Satoh and Jeff Sfakianos and Heike F{\"o}lsch and James Melvin Anderson and Zenta Walther and Ira Mellman},
  journal={Traffic},
  year={2008},
  volume={9 11},
  pages={1915-24}
}
The cell surface proteoglycan, syndecan-1, is essential for normal epithelial morphology and function. Syndecan-1 is selectively localized to the basolateral domain of polarized epithelial cells and interacts with cytosolic PDZ (PSD-95, discs large, ZO-1) domain-containing proteins. Here, we show that the polarity of syndecan-1 is determined by its type II PDZ-binding motif. Mutations within the PDZ-binding motif lead to the mislocalization of syndecan-1 to the apical surface. In contrast to… CONTINUE READING

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