Regulation of CFTR chloride channels by syntaxin and Munc18 isoforms

Anjaparavanda P. Naren, Deborah J. Nelson, Weiwen Xie, Biljana Jovov, Jonathan Pevsner, Mark K. Bennett, Dale J. Benos, Michael W. Quick, Kevin L. Kirk

Research output: Contribution to journalArticle

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 cells. 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 neurosecretion and calcium-channel gating 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-SecI; refs 12-14). Our results indicate that CFTR function in epithelial cells is regulated by an interplay between syntaxin and Munc18 isoforms.

Original languageEnglish (US)
Pages (from-to)302-305
Number of pages4
JournalNature
Volume390
Issue number6657
DOIs
StatePublished - Nov 20 1997

ASJC Scopus subject areas

  • General

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