IndraLab

Statements


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"For B 2 Rs, the peak of the distribution was at ~ 140 nm from that of AKAP150 and KCNQ2 complexes (XREF_FIG, XREF_SUPPLEMENTARY)."

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"Cells co-expressing KCNQ2 and AKAP150 displayed clusters, of which about half represented isolated KCNQ2 homomers, and about half represented KCNQ2 and AKAP150 complexes (XREF_SUPPLEMENTARY)."

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"The nearest-neighbor analysis shows the distribution for KCNQ2-AKAP150 displaying only one sharp and high peak at ~ 20 nm, whereas the distributions for KCNQ2-M 1 Rs or AKAP150-M 1 Rs also displayed a secondary, broader peak at ~ 92 nm, suggesting that not all M 1 Rs are localized in AKAP150 and KCNQ2 complexes."

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"In addition, the binding between KCNQ2 and AKAP150 was also augmented in the presence of calcium, which may have contributed to an increase in CaM retention (XREF_FIG)."

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"We show here that rat KCNQ2 can bind directly to the multivalent A-kinase-anchoring protein AKAP150."

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"Lastly, we noted the large fraction of KCNQ2 and AKAP150 complexes in NG neurons triple labeled for KCNQ2, TRPV1 and AKAP150, nearly identical to the fraction of all three proteins together (XREF_FIG), associations that were again absent in AKAP150 KO mice."

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"Peptides that block AKAP150 binding to the KCNQ2 channel complex antagonize the muscarinic inhibition of the currents."