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 language | English |
|---|---|
| Pages (from-to) | 1915-1924 |
| Number of pages | 10 |
| Journal | Traffic |
| Volume | 9 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - 2008 |
| Externally published | Yes |
Fingerprint
Keywords
- Basolateral
- Epithelia
- PDZ
- Polarity
- Syndecan-1
ASJC Scopus subject areas
- Biochemistry
- Cell Biology
- Structural Biology
- Molecular Biology
- Genetics
Cite this
A PDZ-Binding motif controls basolateral targeting of syndecan-1 along the biosynthetic pathway in polarized epithelial cells. / Maday, Sandra; Anderson, Eric; Chang, Henry C.; Shorter, James; Satoh, Ayano; Sfakianos, Jeff; Fölsch, Heike; Anderson, James M.; Walther, Zenta; Mellman, Ira.
In: Traffic, Vol. 9, No. 11, 2008, p. 1915-1924.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A PDZ-Binding motif controls basolateral targeting of syndecan-1 along the biosynthetic pathway in polarized epithelial cells
AU - Maday, Sandra
AU - Anderson, Eric
AU - Chang, Henry C.
AU - Shorter, James
AU - Satoh, Ayano
AU - Sfakianos, Jeff
AU - Fölsch, Heike
AU - Anderson, James M.
AU - Walther, Zenta
AU - Mellman, Ira
PY - 2008
Y1 - 2008
N2 - 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.
AB - 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.
KW - Basolateral
KW - Epithelia
KW - PDZ
KW - Polarity
KW - Syndecan-1
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UR - http://www.scopus.com/inward/citedby.url?scp=53849147866&partnerID=8YFLogxK
U2 - 10.1111/j.1600-0854.2008.00805.x
DO - 10.1111/j.1600-0854.2008.00805.x
M3 - Article
C2 - 18764819
AN - SCOPUS:53849147866
VL - 9
SP - 1915
EP - 1924
JO - Traffic
JF - Traffic
SN - 1398-9219
IS - 11
ER -