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

Sandra Maday, Eric Anderson, Henry C. Chang, James Shorter, Ayano Satoh, Jeff Sfakianos, Heike Fölsch, James M. Anderson, Zenta Walther, Ira Mellman*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

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 previous examples, however, PDZ-binding motif-dependent polarity is not determined by retention at the basolateral surface but rather by polarized sorting prior to syndecan-1's arrival at the plasma membrane. Although none of the four known PDZ-binding partners of syndecan-1 appears to control basolateral localization, our results show that the PDZ-binding motif of syndecan-1 is decoded along the biosynthetic pathway establishing a potential role for PDZ-mediated interactions in polarized sorting.

Original languageEnglish (US)
Pages (from-to)1915-1924
Number of pages10
JournalTraffic
Volume9
Issue number11
DOIs
StatePublished - 2008

Keywords

  • Basolateral
  • Epithelia
  • PDZ
  • Polarity
  • Syndecan-1

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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