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ABCC8: Physiology and Pathology*

2011 
KATP channels are formed by a K+ conducting, inwardly rectifying pore surrounded by four high or low affinity sulfonylurea receptors, SUR1 or SUR2, respectively, members of the ATP binding cassette (ABC) superfamily that contribute to the regulation of channel activity.1–5 SURs belong to the “C” subfamily of ABC proteins whose members include the multidrug resistance-associated proteins (MRPs), poly-specific efflux pumps, and the cystic fibrosis transmembrane conductance regulator (CFTR), an ATP-gated chloride channel whose dysfunction causes cystic fibrosis, the most common recessive disease in Caucasians. SURs currently have no known transport activity, but are unique among ABC proteins in using ATP binding and/or hydrolysis to regulate the gating of an associated ion conducting pore. KATP channels serve as metabolic sensors and modulate membrane electrical activity in response to changes in cell metabolism. The channels are involved in multiple physiological processes
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