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Physiol. Rev. 78: 227-245, 1998;
0031-9333/98 $15.00
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PHYSIOLOGICAL REVIEWS   Vol. 78 No. 1 January 1998, pp. 227-245
Copyright ©1998 The American Physiological Society

Toward Understanding the Assembly and Structure of KATP Channels

LYDIA AGUILAR-BRYAN, JOHN P. CLEMENT IV, GABRIELA GONZALEZ, KUMUD KUNJILWAR, ANDREY BABENKO, AND JOSEPH BRYAN

Departments of Cell Biology and Medicine, Baylor College of Medicine, Houston, Texas

Aguilar-Bryan, Lydia, John P. Clement IV, Gabriela Gonzalez, Kumud Kunjilwar, Andrey Babenko, and Joseph Bryan. Toward Understanding the Assembly and Structure of KATP Channels. Physiol. Rev. 78: 227-245, 1998. --- Adenosine 5'-triphosphate-sensitive potassium (KATP) channels couple metabolic events to membrane electrical activity in a variety of cell types. The cloning and reconstitution of the subunits of these channels demonstrate they are heteromultimers of inwardly rectifying potassium channel subunits (KIR6.x) and sulfonylurea receptors (SUR), members of the ATP-binding cassette (ABC) superfamily. Recent studies indicate that SUR and KIR6.x associate with 1:1 stoichiometry to assemble a large tetrameric channel, (SUR/KIR6.x)4 . The KIR6.x subunits form the channel pore, whereas SUR is required for activation and regulation. Two KIR6.x genes and two SUR genes have been identified, and combinations of subunits give rise to KATP channel subtypes found in pancreatic beta -cells, neurons, and cardiac, skeletal, and smooth muscle. Mutations in both the SUR1 and KIR6.2 genes have been shown to cause familial hyperinsulinism, indicating the importance of the pancreatic beta -cell channel in the regulation of insulin secretion. The availability of cloned KATP channel genes opens the way for characterization of this family of ion channels and identification of additional genetic defects.






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