Abstract
Epithelial Na+ channels (ENaCs) are activated by extracellular trypsin or by co-expression with channel-activating proteases, although there is no direct evidence that these proteases activate ENaC by cleaving the channel. We previously demonstrated that the α and γ subunits of ENaC are cleaved during maturation near consensus sites for furin cleavage. Using site-specific mutagenesis of channel subunits, ENaC expression in furin-deficient cells, and furin-specific inhibitors, we now report that ENaC cleavage correlates with channel activity. Channel activity in furin-deficient cells was rescued by expression of furin. Our data provide the first example of a vertebrate ion channel that is a substrate for furin and whose activity is dependent on its proteolysis.
Original language | English (US) |
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Pages (from-to) | 18111-18114 |
Number of pages | 4 |
Journal | Journal of Biological Chemistry |
Volume | 279 |
Issue number | 18 |
DOIs | |
State | Published - Apr 30 2004 |
ASJC Scopus subject areas
- Molecular Biology
- Biochemistry
- Cell Biology