IndraLab

Statements

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"Thus, we identified that SUMOylation modulates Kv7.2 and Kv7.3 channel opening by regulating the binding of Kv7.2 with PIP 2 , which is an important mechanism to regulate the M current."
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"Thus, we identified that SUMOylation modulates Kv7.2 and Kv7.3 channel opening by regulating the binding of Kv7.2 with PIP , which is an important mechanism to regulate the M current.The distal Kv7 intracellular C-terminal domain endowed with two coiled coils appears to act as a module for proper channel heteromeric assembly and trafficking as well as a platform for interaction with several regulatory molecules (34, 35)."
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"Our MD simulations indicated that the PIP 2 interaction with the S4-S5 linker of KCNQ2 is not a simple association-dissociation process."
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"The low affinity of PIP bound to KCNQ2 was reported in a previous electrophysiological study which showed that the half-maximal value (EC ) for diC8-PIP on KCNQ2 was ~205 µM ."
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"In fact, in vivo the channel activation is initiated by the depolarization of membrane potential instead of the binding of PIP because the PIP is already bound in KCNQ2."
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"By contrast, none of these experimental conditions (alone or in combination) were able to recover channel function in the case of Kv7.2 subunits incorporating the SLNE-causing variant p.G310Δ10, possibly because of a complete inability of CaM and/or PIP to bind Kv7.2 channels as a consequence of the variant-induced in-frame deletion."
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