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Clathrin is a key regulator of basolateral polarity

Author

Listed:
  • Sylvie Deborde

    (Dyson Vision Research Institute, LC-300, and)

  • Emilie Perret

    (Dyson Vision Research Institute, LC-300, and)

  • Diego Gravotta

    (Dyson Vision Research Institute, LC-300, and)

  • Ami Deora

    (Dyson Vision Research Institute, LC-300, and)

  • Susana Salvarezza

    (Dyson Vision Research Institute, LC-300, and)

  • Ryan Schreiner

    (Dyson Vision Research Institute, LC-300, and)

  • Enrique Rodriguez-Boulan

    (Dyson Vision Research Institute, LC-300, and
    Weill Medical College of Cornell University, 1300 York Avenue, New York, New York 10065, USA)

Abstract

Clathrin-coated vesicles are vehicles for intracellular trafficking in all nucleated cells, from yeasts to humans. Many studies have demonstrated their essential roles in endocytosis and cellular signalling processes at the plasma membrane. By contrast, very few of their non-endocytic trafficking roles are known, the best characterized being the transport of hydrolases from the Golgi complex to the lysosome. Here we show that clathrin is required for polarity of the basolateral plasma membrane proteins in the epithelial cell line MDCK. Clathrin knockdown depolarized most basolateral proteins, by interfering with their biosynthetic delivery and recycling, but did not affect the polarity of apical proteins. Quantitative live imaging showed that chronic and acute clathrin knockdown selectively slowed down the exit of basolateral proteins from the Golgi complex, and promoted their mis-sorting into apical carrier vesicles. Our results demonstrate a broad requirement for clathrin in basolateral protein trafficking in epithelial cells.

Suggested Citation

  • Sylvie Deborde & Emilie Perret & Diego Gravotta & Ami Deora & Susana Salvarezza & Ryan Schreiner & Enrique Rodriguez-Boulan, 2008. "Clathrin is a key regulator of basolateral polarity," Nature, Nature, vol. 452(7188), pages 719-723, April.
    • Handle: RePEc:nat:nature:v:452:y:2008:i:7188:d:10.1038_nature06828
    DOI: 10.1038/nature06828
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