Abstract
The interaction of p11 (annexin II light chain) with the N-terminal domain of Na V1.8, a tetrodotoxin-resistant sodium channel, is essential for the functional expression of the channel. Here we show that p11 binds to Na V1.8 but not to sodium channel isoforms Na V1.2, 1.5, 1.7 or Na V1.9. The binding of amino acids 74–103 of Na V1.8 to p11 residues 33–78 occurs in a random coiled region flanked by two EF hand motifs whose crystal structure has been established. As Na V1.8 channel expression is associated with pain pathways, drugs that disrupt the Na V1.8–p11 interaction and down-regulate channel expression may have analgesic activity.
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