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Received September 21, 2006
Revised October 18, 2006
Accepted after revision October 26, 2006
1 Imperial College London
* To whom correspondence should be addressed. E-mail: a.mathie{at}imperial.ac.uk.
Leak potassium currents in the nervous system are often carried through two pore domain potassium (K2P) channels. These channels are regulated by a number of different G protein coupled receptor (GPCR) pathways. The TASK subfamily of K2P channels are inhibited following activation of the G protein G
q. The mechanism(s) that transduce this inhibition have yet to be established but there is evidence to support a role of PIP2 hydrolysis products, depletion of PIP2, itself, from the membrane, or a direct action of activated Gq on TASK channels. It seems possible that more than one pathway may act in parallel to transduce inhibition. By contrast, TRESK channels are stimulated following activation of Gq. This is due to stimulation of the protein phosphatase, calcineurin, which dephosphorlylates TRESK channels and enhances their activity. TREK channels are the most widely regulated of the K2P channel subfamilies being inhibited following activation of Gq and Gs but enhanced following activation of Gi. The multiple pathways activated and the apparent promiscuous coupling of at least some K2P channel types to different G protein regulatory pathways suggests that the excitability of neurons that express K2P channels will be profoundly sensitive to variations in GPCR activity.
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