Intramolecular interaction of SUR2 subtypes for intracellular ADP-Induced differential control of K(ATP) channels

Circulation Research
Kenji MatsushitaYoshihisa Kurachi

Abstract

ATP-sensitive K+ (K(ATP)) channels are composed of sulfonylurea receptors (SURs) and inwardly rectifying Kir6.2-channels. The C-terminal 42 amino acid residues (C42) of SURs are responsible for ADP-induced differential activation of K(ATP) channels in SUR-subtypes. By examining ADP-effect on K(ATP) channels containing various chimeras of SUR2A and SUR2B, we identified a segment of 7 residues at central portion of C42 critical for this phenomenon. A 3-D structure model of the region containing the second nucleotide-binding domain (NBD2) of SUR and C42 was developed based on the structure of HisP, a nucleotide-binding protein forming the bacterial Histidine transporter complex. In the model, the polar and charged residues in the critical segment located within a distance that allows their electrostatic interaction with Arg1344 at the Walker-A loop of NBD2. Therefore, the interaction might be involved in the control of ADP-induced differential activation of SUR2-subtype K(ATP) channels.

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Citations

Jan 25, 2007·Nature Clinical Practice. Cardiovascular Medicine·Timothy M OlsonAndre Terzic
Mar 11, 2003·Journal of Cardiovascular Electrophysiology·William C Cole, Odile Clément-Chomienne
Sep 25, 2002·Proceedings of the National Academy of Sciences of the United States of America·Leonid V ZingmanAndre Terzic
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May 25, 2005·Journal of Molecular and Cellular Cardiology·Christophe MoreauMichel Vivaudou
Oct 20, 2012·Biochemistry·Jorge P López-AlonsoVoula Kanelis
Jan 31, 2006·FEBS Letters·Annie Frelet, Markus Klein
Jul 21, 2007·Journal of Applied Physiology·L V ZingmanA Terzic
Jan 21, 2010·Physiological Reviews·Hiroshi HibinoYoshihisa Kurachi
Dec 22, 2004·The Journal of Immunology : Official Journal of the American Association of Immunologists·Sarah EhsesMichael R Knittler

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