IndraLab

Statements

CALM binds KCNQ2 and IQ. 6 / 6
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"Since inhibition of CaM binding to the IQ motif of KCNQ2 completely blocks the targeting of heteromeric HA-KCNQ3/KCNQ2 channels from the ER to the axonal surface ( xref – xref ), the KCNQ2 subunits with de novo xref – xref and BFNC xref mutations in the IQ motif would likely exert a dominant negative effect by forming channels with KCNQ3 and retaining them in the ER."
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"These results collectively support the idea that disruption of CaM binding to the IQ motif of KCNQ2 retains intact heteromeric channels in the ER of cultured hippocampal neurons."
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"By utilizing a dominant-negative mutant CaM that is unable to bind Ca 2+ xref or mutations that block or reduce CaM binding xref , xref , we show that CaM interaction with the IQ motif of KCNQ2 is required for exit of KCNQ channels from the endoplasmic reticulum (ER), and their subsequent enrichment at the axonal plasma membranes in cultured hippocampal neurons."
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"These results reflect the differences in the axonal enrichment of wild-type and A343D mutant channels, further supporting a critical role for CaM interaction with the IQ motif of KCNQ2 in regulating axonal surface expression of intact KCNQ channels."
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"Our results with CD4-Q2C proteins ( xref – xref ) suggest that enrichment of intact KCNQ channels at the axonal surface may be mediated by CaM interaction with the IQ motif of KCNQ2."
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"These correlative findings suggest that enrichment of CD4-Q2C and HA-KCNQ3/KCNQ2 channels at the axonal surface requires CaM interaction with the IQ motif of KCNQ2."
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