Article
A PDZ-binding motif controls basolateral targeting of syndecan-1 along the biosynthetic pathway in polarized epithelial cells.
Traffic (Copenhagen, Denmark) - 1 Nov 2008
Maday Sandra, Anderson Eric, Chang Henry C, Shorter James, Satoh Ayano, Sfakianos Jeff, Fölsch Heike, Anderson James M, Walther Zenta, Mellman Ira
Abstract excerpt
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...
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