IndraLab

Statements

Dclk3 activates KCNMA1. 11 / 11
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"These studies indicate that CLR at 30-50 mol% modulates BK channel activity in absence of the complex proteolipid organization that is characteristic of natural membranes."
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"Moreover, in absence of Ca 2+ , BK channel-activating concentrations of Mg 2+ (10 mM) did not support CLR action."
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"Studies of CLR modulation of BK channel pharmacology, however, seem to be restricted to the CLR-alcohol (ethyl alcohol, ethanol) interaction on channel function."
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"Studies on BK channel forming recombinant proteins reconstituted into artificial bilayers of simple composition demonstrate that a planar binary phospholipid bilayer suffices to support CLR modulation of BK channel steady-state activity."
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"Thus, CLR modulation of BK channel function may occur in absence of cytosolic signaling, intracellular organelles, caveolae organization and even a complex bilayer lipid composition."
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"The current chapter reviews the literature documenting CLR modulation of BK channel function at a variety of levels ranging from organ systems to artificial lipid bilayers."
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"Identification of a slo1 protein site for CLR could lead to identification of polymorphisms in human populations that would be more and less susceptible to CLR modulation of BK channel function."
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"In neurons, CLR modulation of BK channel activity has been linked to plastic changes that occur in the neuronal membrane in response to protracted or repeated alcohol exposure."
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"Second, protein mediated and lipid mediated interactions could independently contribute to CLR modulation of BK channel function, as reported for the oxytocin receptor and its structurally related brain cholecystokinin receptor."
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"Several studies have attributed CLR dependent modulation of BK channel activity in native cellular membranes to BK channel clustering in membrane rafts."
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"Interestingly, cannabinoid induced potentiation of slo1 current is lost after membrane CLR depletion and restored upon CLR repletion, with the slo1 CTD providing several CLR-recognition domains that mediate CLR modulation of slo1 activity (see below)."
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