IndraLab

Statements

Dclk3 inhibits KCNMA1. 11 / 11
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"Other possibilities can not be excluded : CLR antagonism of slo1 channel potentiation by ethanol may be attributed to CLR making it more difficult for ethanol molecules to partition into the bilayer and thus reaching eventual channel subunit targets."
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"This result indicates that the CTD is necessary for CLR inhibition of BK channel activity."
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"Because the maintenance of caveolae depends on not only caveolin-1 and associated proteins but also on free CLR levels in the membrane, the modification of BK current by CLR depleting treatment can be explained by the loss of direct BK channel inhibition by CLR (Sections 4.3.1 and 4.3.2), and/or by alteration of local raft organization with disruption of interactions between BK and raft components, caveolin-1 in particular."
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"Electrophysiological data following cbv1 channel reconstitution into POPE : POPS (3:1 w/w) bilayers reveal that the channel forming subunit is sufficient to sustain CLR inhibition of BK channel steady-state activity."
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"Therefore, BK channel inhibition by CLR selectively requires optimal levels of Ca 2+ being recognized by either of the slo1 high-affinity Ca 2+ -sensing sites."
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"In synthesis, it is extremely unlikely that modification of a single physical property of the lipid bilayer is the only mechanism determining CLR inhibition of BK channel activity."
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"Data obtained after reconstitution of homomeric hslo1 channels into 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE) : 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphol-serine sodium salt (POPS) (3:1 w/w) lipid bilayers first demonstrated that CLR inhibition of BK channel steady-state activity, previously reported with native channel in natural membranes (Section 3) was sustained in a bare proteolipid environment nominally composed of two phospholipid species and the channel forming hslo1 subunit."
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"Even at the phenomenological level, CLR and ethanol actions on BK channels differ in two basic aspects : 1) ethanol action on is critically modulated by accessory beta1 subunits whereas CLR action is not, and 2) ethanol action on slo1 channel activity requires, and is a function of, activating Ca 2+ i whereas CLR inhibition of slo1 activity does not."
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"A simpler and more plausible explanation is that cbv1 itself contains a site (s) for CLR sensing that is responsible for CLR reduction of BK channel activity (Section 4.3.2)."
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"These similarities underscore that neither the complex cytoarchitecture of cell membranes nor the continuous presence of cell signaling is required for CLR induced inhibition of BK channel activity."
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"Therefore, it is very unlikely that changes in bilayer thickness provide a major mechanism underlying CLR inhibition of BK channel activity."
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