Overslaan en naar de inhoud gaan
Publicaties | Personen | Instituten | Projecten
[ meld een fout in dit record ]mandje (1): toevoegen | toon Print deze pagina

one publication added to basket [238740]
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
Peer reviewed article  

Beschikbaar in  Auteurs 

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.

Alle informatie in het Integrated Marine Information System (IMIS) valt onder het VLIZ Privacy beleid Top | Auteurs