Gp135/podocalyxin and NHERF-2 participate in the formation of a preapical domain during polarization of MDCK cells
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- Doris Meder
- Max Planck Institute of Molecular Cell Biology and Genetics, D-01307 Dresden, Germany
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- Anna Shevchenko
- Max Planck Institute of Molecular Cell Biology and Genetics, D-01307 Dresden, Germany
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- Kai Simons
- Max Planck Institute of Molecular Cell Biology and Genetics, D-01307 Dresden, Germany
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- Joachim Füllekrug
- Max Planck Institute of Molecular Cell Biology and Genetics, D-01307 Dresden, Germany
抄録
<jats:p>Epithelial polarization involves the segregation of apical and basolateral membrane domains, which are stabilized and maintained by tight junctions and membrane traffic. We report that unlike most apical and basolateral proteins in MDCK cells, which separate only after junctions have formed, the apical marker gp135 signifies an early level of polarized membrane organization established already in single cells. We identified gp135 as the dog orthologue of podocalyxin. With a series of domain mutants we show that the COOH-terminal PSD-95/Dlg/ZO-1 (PDZ)–binding motif is targeting podocalyxin to the free surface of single cells as well as to a subdomain of the terminally polarized apical membrane. This special localization of podocalyxin is shared by the cytoplasmic PDZ-protein Na+/H+ exchanger regulatory factor (NHERF)-2. Depleting podocalyxin by RNA interference caused defects in epithelial polarization. Together, our data suggest that podocalyxin and NHERF-2 function in epithelial polarization by contributing to an early apical scaffold based on PDZ domain-mediated interactions.</jats:p>
収録刊行物
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- The Journal of Cell Biology
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The Journal of Cell Biology 168 (2), 303-313, 2005-01-10
Rockefeller University Press
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キーワード
詳細情報 詳細情報について
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- CRID
- 1361137043882865536
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- ISSN
- 15408140
- 00219525
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- データソース種別
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- Crossref