Over het archief
Het OWA, het open archief van het Waterbouwkundig Laboratorium heeft tot doel alle vrij toegankelijke onderzoeksresultaten van dit instituut in digitale vorm aan te bieden. Op die manier wil het de zichtbaarheid, verspreiding en gebruik van deze onderzoeksresultaten, alsook de wetenschappelijke communicatie maximaal bevorderen.
Dit archief wordt uitgebouwd en beheerd volgens de principes van de Open Access Movement, en het daaruit ontstane Open Archives Initiative.
Basisinformatie over ‘Open Access to scholarly information'.
Up- and down-regulation of the mechano-gated K2P channel TREK-1 by PIP2 and other membrane phospholipids
Chemin, J.; Patel, A.J.; Duprat, F.; Sachs, F.; Lazdunski, M.; Honoré, E. (2007). Up- and down-regulation of the mechano-gated K2P channel TREK-1 by PIP2 and other membrane phospholipids. Pflügers Arch. Eur. J. Physiol. 455(1): 97-103. http://dx.doi.org/10.1007/s00424-007-0250-2
In: Pflügers Archiv - European Journal of Physiology. Springer: Berlin. ISSN 0031-6768; e-ISSN 1432-2013, meer
| |
Auteurs | | Top |
- Chemin, J.
- Patel, A.J.
- Duprat, F.
|
- Sachs, F.
- Lazdunski, M.
- Honoré, E., meer
|
|
Abstract |
TREK-1 is an unconventional K+ channel that is activated by both physical and chemical stimuli. In this study, we show that the inner leaflet membrane phospholipids, including PIP2, exert a mixed stimulatory and inhibitory effect on TREK-1. Intra-cellular phospholipids inhibit basal channel activity and activation by membrane stretch, intra-cellular acidosis and arachidonic acid. However, binding of endogenous negative inner leaflet phospholipids with poly-lysine reduces inhibition and reveals channel stimulation by exogenous intra-cellular phospholipids. A similar effect is observed with PI, PE, PS and PA, unlike DG, demonstrating that the phosphate at position 3 is required although the global charge of the molecule is not critical. Inhibition depends on the distal C-terminal domain that conditions channel mechano-sensitivity, but is independent of the positively charged PIP2 stimulatory site in the proximal C-terminal domain. This is, to our knowledge, the first report of an ion channel dually regulated by membrane phospholipids. |
IMIS is ontwikkeld en wordt gehost door het VLIZ.