Title |
ABCC8 and ABCC9: ABC transporters that regulate K+ channels
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Published in |
Pflügers Archiv - European Journal of Physiology, August 2006
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DOI | 10.1007/s00424-006-0116-z |
Pubmed ID | |
Authors |
Joseph Bryan, Alvaro Muñoz, Xinna Zhang, Martina Düfer, Gisela Drews, Peter Krippeit-Drews, Lydia Aguilar-Bryan |
Abstract |
The sulfonylurea receptors (SURs) ABCC8/SUR1 and ABCC9/SUR2 are members of the C-branch of the transport adenosine triphosphatase superfamily. Unlike their brethren, the SURs have no identified transport function; instead, evolution has matched these molecules with K(+) selective pores, either K(IR)6.1/KCNJ8 or K(IR)6.2/KCNJ11, to assemble adenosine triphosphate (ATP)-sensitive K(+) channels found in endocrine cells, neurons, and both smooth and striated muscle. Adenine nucleotides, the major regulators of ATP-sensitive K(+) (K(ATP)) channel activity, exert a dual action. Nucleotide binding to the pore reduces the activity or channel open probability, whereas Mg-nucleotide binding and/or hydrolysis in the nucleotide-binding domains of SUR antagonize this inhibitory action to stimulate channel openings. Mutations in either subunit can alter this balance and, in the case of the SUR1/KIR6.2 channels found in neurons and insulin-secreting pancreatic beta cells, are the cause of monogenic forms of hyperinsulinemic hypoglycemia and neonatal diabetes. Additionally, the subtle dysregulation of K(ATP) channel activity by a K(IR)6.2 polymorphism has been suggested as a predisposing factor in type 2 diabetes mellitus. Studies on K(ATP) channel null mice are clarifying the roles of these metabolically sensitive channels in a variety of tissues. |
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Demographic breakdown
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Student > Ph. D. Student | 22 | 22% |
Student > Master | 10 | 10% |
Other | 9 | 9% |
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Other | 14 | 14% |
Unknown | 16 | 16% |
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Chemistry | 3 | 3% |
Other | 10 | 10% |
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