IndraLab

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Phosphatidylinositol phosphate activates KCNMA1. 9 / 9
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"However, an essential role of the GR domain may be excluded, at least in our experimental conditions, because the truncated Slo1 channel without the GR domain can be robustly stimulated by PIP 2 when coexpressed with beta1."
25825171
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"PIP 2 clearly decreased macroscopic currents through Slo1 and Slo1 + gamma1 but increased macroscopic currents through Slo1 + beta1 and Slo1 + beta4 (XREF_FIG)."
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"Previous findings demonstrated that metabolic products of PIP 2 and downstream targets such as PLC, ryanodine receptors, kinases, and free fatty acids modulate BK channel activity."
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"Additionally, activation of lipid kinases via Mg-ATP increases membrane PIP 2 levels and thus modulates BK channel activity."
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"Moreover, the differential expression of BK accessory subunits across tissues raises the possibility that a direct PIP 2 modulation of BK channel function is specifically relevant in tissues where the beta 1 subunit is highly expressed."
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"Therefore, the sequence RKK in the cbv1 S6-S7 linker is involved in PIP 2 activation of the BK channel."
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"In the absence of Ca 2+ at very negative voltages where the VSDs are mostly at rest, PIP 2 increased P o in both Slo1 (XREF_FIG) and Slo1 + beta1 (XREF_FIG), and the fractional increases were indistinguishable between the two channel types (P = 0.955; XREF_FIG), despite the contrasting effects at more positive voltages where VSD activation and G/G max are appreciable."
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"Two distinct effects of PIP 2 underlie auxiliary subunit dependent modulation of Slo1 BK channels."
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"In spite of the key roles of PIP 2 and BK channels in cell excitability and signaling, it remains unknown whether PIP 2 can directly modulate BK channel function."
18562499