Rapid Chemically Induced Changes of PtdIns(4,5)P2 Gate KCNQ Ion Channels.

@article{citeulike:895560, abstract = {To resolve 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 PtdIns(4,5)P2 is depleted without changing Ca(2+), diacylglycerol, or InsP3. Current rises by 30\% when PtdIns(4,5)P2 is overproduced and does not change when PtdIns(3,4,5)P3 is raised. Hence depletion of PtdIns(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.}, address = {Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle, WA 98195, USA.}, author = {Suh, Byung-Chang C. and Inoue, Takanari and Meyer, Tobias and Hille, Bertil }, citeulike-article-id = {895560}, comment = {A way to selectively and immediately change PdtIns(4,5)P2 levels in cells. Involves transfection of two constructs + dimerization of the two with a chemical compound.}, doi = {10.1126/science.1131163}, issn = {1095-9203}, journal = {Science}, keywords = {fluorescent\_proteins, journal\_club, lipids, live\_cell\_imaging, signaling\_pathways, technique}, month = {September}, posted-at = {2006-10-13 17:21:28}, priority = {0}, title = {Rapid Chemically Induced Changes of PtdIns(4,5)P2 Gate KCNQ Ion Channels.}, url = {http://dx.doi.org/10.1126/science.1131163}, year = {2006} }

TY - JOUR ID - citeulike:895560 L3 - citeulike-article-id:895560 TI - Rapid Chemically Induced Changes of PtdIns(4,5)P2 Gate KCNQ Ion Channels. JF - Science AD - Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle, WA 98195, USA. SN - 1095-9203 N2 - To resolve 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 PtdIns(4,5)P2 is depleted without changing Ca(2+), diacylglycerol, or InsP3. Current rises by 30% when PtdIns(4,5)P2 is overproduced and does not change when PtdIns(3,4,5)P3 is raised. Hence depletion of PtdIns(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. KW - fluorescent_proteins KW - journal_club KW - lipids KW - live_cell_imaging KW - signaling_pathways KW - technique N1 - A way to selectively and immediately change PdtIns(4,5)P2 levels in cells. Involves transfection of two constructs + dimerization of the two with a chemical compound. AU - Suh, Byung-Chang AU - Inoue, Takanari AU - Meyer, Tobias AU - Hille, Bertil PY - 2006/09/21/ UR - http://dx.doi.org/10.1126/science.1131163 ER -