Rapid chemically induced changes of PtdIns(4,5)P2 gate KCNQ ion channels |
| |
Authors: | Suh Byung-Chang Inoue Takanari Meyer Tobias Hille Bertil |
| |
Affiliation: | Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle, WA 98195, USA. |
| |
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)P2 or PI(4,5)P2] is depleted without changing Ca2+, 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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|