Intramolecular Interaction of SUR2 Subtypes for Intracellular ADP-Induced Differential Control of KATP Channels

ATP-sensitive K (KATP) 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 KATP channels in SUR-subtypes. By examining ADP-effect on KATP channel...

Full description

Saved in:
Bibliographic Details
Published inCirculation research Vol. 90; no. 5; pp. 554 - 561
Main Authors Matsushita, Kenji, Kinoshita, Kengo, Matsuoka, Tetsuro, Fujita, Akikazu, Fujikado, Takashi, Tano, Yasuo, Nakamura, Haruki, Kurachi, Yoshihisa
Format Journal Article
LanguageEnglish
Published Hagerstown, MD American Heart Association, Inc 22.03.2002
Lippincott
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:ATP-sensitive K (KATP) 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 KATP channels in SUR-subtypes. By examining ADP-effect on KATP 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 KATP channels.
ISSN:0009-7330
1524-4571
DOI:10.1161/01.RES.0000012666.42782.30