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Regulation of CFTR chloride channels by syntaxin and Munc18 isoforms

Author

Listed:
  • Anjaparavanda P. Naren

    (Gregory Fleming James Cystic Fibrosis Research Center)

  • Deborah J. Nelson

    (University of Chicago)

  • Weiwen Xie

    (University of Chicago)

  • Biljana Jovov

    (Gregory Fleming James Cystic Fibrosis Research Center)

  • Jonathan Pevsner

    (Kennedy Krieger Institute and The Johns Hopkins University School of Medicine)

  • Mark K. Bennett

    (University of California)

  • Dale J. Benos

    (Gregory Fleming James Cystic Fibrosis Research Center)

  • Michael W. Quick

    (University of Alabama at Birmingham)

  • Kevin L. Kirk

    (Gregory Fleming James Cystic Fibrosis Research Center)

Abstract

The cystic fibrosis gene encodes a cyclic AMP-gated chloride channel (CFTR) that mediates electrolyte transport across the luminal surfaces of a variety of epithelial cells1,2,3,4. The molecular mechanisms that modulate CFTR activity in epithelial tissues are poorly understood. Here we show that CFTR is regulated by an epithelially expressed syntaxin (syntaxin 1A), a membrane protein that also modulates neurosecretion5,6,7 and calcium-channel gating8,9,10,11 in brain. Syntaxin 1A physically interacts with CFTR chloride channels and regulates CFTR-mediated currents both in Xenopus oocytes and in epithelial cells that normally express these proteins. The physical and functional interactions between syntaxin 1A and CFTR are blocked by a syntaxin-binding protein of the Munc18 protein family (also called n-Sec1; refs 12,13,14). Our results indicate that CFTR function in epithelial cells is regulated by an interplay between syntaxin and Munc18 isoforms.

Suggested Citation

  • Anjaparavanda P. Naren & Deborah J. Nelson & Weiwen Xie & Biljana Jovov & Jonathan Pevsner & Mark K. Bennett & Dale J. Benos & Michael W. Quick & Kevin L. Kirk, 1997. "Regulation of CFTR chloride channels by syntaxin and Munc18 isoforms," Nature, Nature, vol. 390(6657), pages 302-305, November.
    • Handle: RePEc:nat:nature:v:390:y:1997:i:6657:d:10.1038_36882
    DOI: 10.1038/36882
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