The protein kinase A-regulated cardiac Cl- channel resembles the cystic fibrosis transmembrane conductance regulator

Article Abstract:

The phosphorylation of AMP-dependent protein kinase (PKA) in cardiac myocytes yields chloride channels that are virtually indistinguishable from cystic fibrosis transmembrane conductance regulator (CTFR), another chloride channel that is abnormal in people with cystic fibrosis. Mutual possession of such characteristics as voltage-independent gating and low single-channel conductance proved the similarity between PKA and CTFR. This finding may open the way for further discoveries concerning the pathophysiology of cystic fibrosis.

Abnormalities, Physiological aspects, Protein kinases, Heart cells

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CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains

Article Abstract:

Single-channel recording methods are used on intact cystic fibrosis transmembrane conductance regulator (CFTR) molecules to directly follow opening and closing of channel gates, and the occurrences are related to ATP-mediated events in the nucleotide binding domains (NBDs). It was found that energetic coupling between two CFTR residues, expected to lie on opposite sides of its predicted NDB1-NBD2 dimer interface, changes in concert with channel gating status.

United States, Biological Product (except Diagnostic) Manufacturing, Nucleic Acid Derivatives, Adenosine triphosphate, ATP, Nucleotides

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The ABC protein turned chloride channel whose failure causes cystic fibrosis

Article Abstract:

CFTR chloride channels, which belong to the superfamily of ABC transporter ATPases, are encoded by the gene mutated by ATP-driven conformational changes, in patients with cystic fibrosis. Structural and biochemical information from prokaryotic ABC proteins and functional information from CFTR channels leads to a unifying mechanism explaining those ATP-driven conformational changes.

Health aspects, Risk factors, Adenosine triphosphatase, ATPases

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