The structural integrity of the second coiled-coil motif in the KCNQ2 subunit interaction domain is crucial for its autonomous folding and assembly into tetramers.
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May guide mechanistic research on KCNQ2 assembly; leaves open any clinical translation in channelopathies.
Mutations in the KCNQ2 gene cause myokymia and neonatal epilepsy, indicating that this K(+) channel regulates the excitability of lower motoneurons and CNS neurons. Little is known about the parameters that direct the assembly of this multimeric molecule and other KCNQ subunits. Here, we show that the carboxy-terminal subunit interaction domain of KCNQ2 autonomously folds and assembles into tetramers. This domain contains a bipartite coiled-coil motif. Whereas structural integrity of the second coiled-coil motif is crucial for tetramer formation, that of the first motif is less important. These data suggest a crucial role of coiled-coil motifs in tetrameric KCNQ channel assembly.
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Wehling et al. (2007) studied this question.
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