• Media type: E-Article
  • Title: PIP 2 and PIP as Determinants for ATP Inhibition of K ATP Channels
  • Contributor: Baukrowitz, Thomas; Schulte, Uwe; Oliver, Dominik; Herlitze, Stefan; Krauter, Tobias; Tucker, Stephen J.; Ruppersberg, J. Peter; Fakler, Bernd
  • imprint: American Association for the Advancement of Science (AAAS), 1998
  • Published in: Science
  • Language: English
  • DOI: 10.1126/science.282.5391.1141
  • ISSN: 0036-8075; 1095-9203
  • Origination:
  • Footnote:
  • Description: <jats:p> Adenosine triphosphate (ATP)–sensitive potassium (K <jats:sub>ATP</jats:sub> ) channels couple electrical activity to cellular metabolism through their inhibition by intracellular ATP. ATP inhibition of K <jats:sub>ATP</jats:sub> channels varies among tissues and is affected by the metabolic and regulatory state of individual cells, suggesting involvement of endogenous factors. It is reported here that phosphatidylinositol-4,5-bisphosphate (PIP <jats:sub>2</jats:sub> ) and phosphatidylinositol-4-phosphate (PIP) controlled ATP inhibition of cloned K <jats:sub>ATP</jats:sub> channels (K <jats:sub>ir</jats:sub> 6.2 and SUR1). These phospholipids acted on the K <jats:sub>ir</jats:sub> 6.2 subunit and shifted ATP sensitivity by several orders of magnitude. Receptor-mediated activation of phospholipase C resulted in inhibition of K <jats:sub>ATP</jats:sub> -mediated currents. These results represent a mechanism for control of excitability through phospholipids. </jats:p>