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Significance Ion channels are protein pores that pass ions across biological membranes. CFTR is an anion channel required for proper salt–water transport across epithelia, including the lung and the gut. CFTR overactivation due to bacterial toxins causes severe diarrhea (e.g., in cholera), and impaired activation due to mutations underlies cystic fibrosis, a lethal disease. CFTR is activated by a kinase (PKA) which phosphorylates the channel. Here we show that CFTR activation is not caused by phosphorylation, as believed, but by simple PKA binding which promotes reversible release of CFTR’s regulatory (R) domain from an inhibitory position. Subsequent R-domain phosphorylation renders activation irreversible. Reversible channel activation is likely mediated by several members of a large protein network that interacts with CFTR.

Simple binding of protein kinase A prior to phosphorylation allows CFTR anion channels to be opened by nucleotides