Nucleoside triphosphates are required to open the CFTR chloride channel

The CFTR Cl− channel contains two predicted nucleotide-binding domains (NBD1 and NBD2); therefore, we examined the effect of ATP on channel activity. Once phosphorylated by cAMP-dependent protein kinase (PKA), channels required cytosolic ATP to open. Activation occurred by a PKA-independent mechanis...

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Veröffentlicht in:	Cell 1991-11, Vol.67 (4), p.775-784
Hauptverfasser:	Anderson, Matthew P., Berger, Herbert A., Rich, Devra P., Gregory, Richard J., Smith, Alan E., Welsh, Michael J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - analogs & derivatives Adenosine Triphosphate - pharmacology Adenosine Triphosphate - physiology Animals ATP Binding Sites Biological and medical sciences Cell membranes. Ionic channels. Membrane pores Cell structures and functions chloride Chloride Channels Cystic Fibrosis Transmembrane Conductance Regulator DNA Mutational Analysis Electric Conductivity Fundamental and applied biological sciences. Psychology Humans In Vitro Techniques Ion Channel Gating Membrane Proteins - physiology Mice Molecular and cellular biology Nucleotides - physiology Phosphorylation Protein Kinases - physiology Structure-Activity Relationship transmembrane conductance regulator
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