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Statements

SLC5A3 binds KCNQ2. 3 / 3
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"In particular, the ancillary subunit KCNE4, which our PLA experiments show interacts with SMIT1 in VSMCs, coassembles with Kv7 channels and alters their function. xref Because KCNE subunits modulate the binding of SMIT1 to Kv7.2, xref the possibility exists that the lack of effect of SMIT1 overexpression in CHO cells was due to the absence of KCNE4 subunits that could modify SMIT1 interaction with the Kv7.4/Kv7.5 channels."
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"Consistent with this hypothesis, KCNQ3 * –SMIT1 but not KCNQ2–SMIT1 was responsive to GABA, with the functional output being an approximately twofold reduction in SMIT1 myo -inositol uptake (Fig.  xref ), similar to effects of GABA on KCNQ2/3–SMIT1 complexes (Fig.  xref )."
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"Importantly, the ability of SMIT1 to be upregulated by an extracellular hypertonic solution via the transcription factor tonicity-responsive enhancer binding protein (TonEBP) effectively coupled KCNQ2 electrical activity, and thus membrane excitability, to osmotic potential – suggested to be the physiological role for the functional interaction between KCNQ2 and SMIT1, via a downstream product of SMITI-transported myo -inositol, PIP 2 [ xref ]."
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