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A PDZ‐Binding Motif Controls Basolateral Targeting of Syndecan‐1 Along the Biosynthetic Pathway in Polarized Epithelial Cells
Author(s) -
Maday Sandra,
Anderson Eric,
Chang Henry C.,
Shorter James,
Satoh Ayano,
Sfakianos Jeff,
Fölsch Heike,
Anderson James M.,
Walther Zenta,
Mellman Ira
Publication year - 2008
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2008.00805.x
Subject(s) - pdz domain , syndecan 1 , microbiology and biotechnology , cell polarity , biology , epithelial polarity , cytoplasm , scaffold protein , plasma protein binding , cell , signal transduction , biochemistry
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.