Rapid chemically induced changes of PtdIns(4,5)P2 gate KCNQ ion channels

Byung Chang Suh, Takanari Inoue, Tobias Meyer, Bertil Hille

Research output: Contribution to journalArticlepeer-review

Abstract

To resolve the controversy about messengers regulating KCNQ ion channels during phospholipase C-mediated suppression of current, we designed translocatable enzymes that quickly alter the phosphoinositide composition of the plasma membrane after application of a chemical cue. The KCNQ current falls rapidly to zero when phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P 2 or PI(4,5)P2] is depleted without changing Ca 2+, diacylglycerol, or inositol 1,4,5-trisphosphate. Current rises by 30% when PI(4,5)P2 is overproduced and does not change when phosphatidylinositol 3,4,5-trisphosphate is raised. Hence, the depletion of PI(4,5)P2 suffices to suppress current fully, and other second messengers are not needed. Our approach is ideally suited to study biological signaling networks involving membrane phosphoinositides.

Original languageEnglish (US)
Pages (from-to)1454-1457
Number of pages4
JournalScience
Volume314
Issue number5804
DOIs
StatePublished - Dec 1 2006
Externally publishedYes

ASJC Scopus subject areas

  • General

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