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A PDZ-Binding Motif Controls Basolateral Targeting of Syndecan-1 Along the Biosynthetic Pathway in Polarized Epithelial Cells
Article first published online: 30 JUL 2008
DOI: 10.1111/j.1600-0854.2008.00805.x
© 2008 The Authors. Journal compilation © 2008 Blackwell Munksgaard
Additional Information
How to Cite
Maday, S., Anderson, E., Chang, H. C., Shorter, J., Satoh, A., Sfakianos, J., Fölsch, H., Anderson, J. M., Walther, Z. and Mellman, I. (2008), A PDZ-Binding Motif Controls Basolateral Targeting of Syndecan-1 Along the Biosynthetic Pathway in Polarized Epithelial Cells. Traffic, 9: 1915–1924. doi: 10.1111/j.1600-0854.2008.00805.x
Publication History
- Issue published online: 10 OCT 2008
- Article first published online: 30 JUL 2008
- Received 4 February 2008, revised and accepted for publication 24 July 2008, uncorrected manuscript published online 30 July 2008
Keywords:
- basolateral;
- epithelia;
- PDZ;
- polarity;
- syndecan-1
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.