Abstract
Voltage-gated potassium (Kv) channels open in response to changes in membrane potential to permit passage of K(+) ions across the cell membrane, down their electrochemical gradient. Sodium-coupled solute transporters utilize the downhill sodium gradient to co-transport solutes, ranging from ions to sugars to neurotransmitters, into the cell. A variety of recent studies have uncovered cooperation between these two structurally and functionally unrelated classes of protein, revealing previously unnoticed functional crosstalk and in many cases physical interaction to form channel-transporter (chansporter) complexes. Adding to this field, Bartolomé-Martín and colleagues now report that the heteromeric KCNQ2/KCNQ3 (Kv7.2/7.3) potassium channel - the primary molecular correlate of the neuronal M-current - can physically interact with two sodium-coupled neurotransmitter transporters expressed in the brain, DAT and GLT1 (dopamine and glutamate transporters, respectively). The authors provide evidence that the interactions may enhance transporter activity while dampening the depolarizing effects of sodium influx. Cumulative evidence discussed here suggests that chansporter complexes represent a widespread form of cellular signaling hub, in the CNS and other tissues. This article is part of the issue entitled 'Special Issue on Neurotransmitter Transporters'.