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PIP2 and PIP as determinants for ATP inhibition of KATP channels.

Authors
  • Baukrowitz, T
  • Schulte, U
  • Oliver, D
  • Herlitze, S
  • Krauter, T
  • Tucker, S J
  • Ruppersberg, J P
  • Fakler, B
Type
Published Article
Journal
Science (New York, N.Y.)
Publication Date
Nov 06, 1998
Volume
282
Issue
5391
Pages
1141–1144
Identifiers
PMID: 9804555
Source
Medline
License
Unknown

Abstract

Adenosine triphosphate (ATP)-sensitive potassium (KATP) channels couple electrical activity to cellular metabolism through their inhibition by intracellular ATP. ATP inhibition of KATP 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 (PIP2) and phosphatidylinositol-4-phosphate (PIP) controlled ATP inhibition of cloned KATP channels (Kir6.2 and SUR1). These phospholipids acted on the Kir6.2 subunit and shifted ATP sensitivity by several orders of magnitude. Receptor-mediated activation of phospholipase C resulted in inhibition of KATP-mediated currents. These results represent a mechanism for control of excitability through phospholipids.

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