Cloning and expression of an inwardly rectifying ATP-regulated potassium channel

• Published in: Nature (London) Vol. 362; no. 6415; pp. 31 - 38
• Main Authors: Ho, Kevin, Nichols, Colin G, Lederer, W. Jonathan, Lytton, Jonathan, Vassilev, Peter M, Kanazirska, Marie V, Hebert, Steven C
• Format: Journal Article
• Language: English
• Published: London Nature Publishing 04.03.1993; Nature Publishing Group
• Subjects: Adenosine Triphosphate - pharmacology; Amino Acid Sequence; Animals; ATP; Barium - pharmacology; Barium Compounds; Base Sequence; Biochemistry; Biological and medical sciences; cDNA; Cell Membrane - physiology; Cell Membrane - ultrastructure; channels; Chlorides; Cloning; Cloning, Molecular; Deoxyribonucleic acid; DNA; expression; Female; Fundamental and applied biological sciences. Psychology; genes; Genes. Genome; Ion Channel Gating; kidney; Kidney Medulla - physiology; Membrane Potentials - drug effects; Models, Structural; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; nucleotide sequence; Oocytes - drug effects; Oocytes - physiology; Open Reading Frames; Poly A - genetics; Potassium; Potassium Channels - drug effects; Potassium Channels - genetics; Potassium Channels - physiology; Protein Conformation; Protein Structure, Secondary; Rats; regulation; RNA - genetics; RNA, Messenger - genetics; RNA, Messenger - metabolism; Second Messenger Systems; Sequence Homology, Amino Acid; Structural engineering; Xenopus laevis; Membrane protein; Electrophysiology; Primary structure; Ionic channel; Molecular cloning; Gating; Potassium; Voltage clamp method
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/362031a0

A complementary DNA encoding an ATP-regulated potassium channel has been isolated by expression cloning from rat kidney. The predicted 45K protein, which features two potential membrane-spanning helices and a proposed ATP-binding domain, represents a major departure from the basic structural design characteristic of voltage-gated and second messenger-gated ion channels. But the presence of an H5 region, which is likely to form the ion conduction pathway, indicates that the protein may share a common origin with voltage-gated potassium channel proteins.