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Voltage-gated potassium (K + ) channels are present in all living systems. Despite high structural similarities in the transmembrane domains (TMD), this K +  channel type segregates into at least two main functional categories—hyperpolarization-activated, inward-rectifying (K in ) and depolarization-activated, outward-rectifying (K out ) channels. Voltage-gated K +  channels sense the membrane voltage via a voltage-sensing domain that is connected to the conduction pathway of the channel. It has been shown that the voltage-sensing mechanism is the same in K in  and K out  channels, but its performance results in opposite pore conformations. It is not known how the different coupling of voltage-sensor and pore is implemented. Here, we studied sequence and structural data of voltage-gated K +  channels from animals and plants with emphasis on the property of opposite rectification. We identified structural hotspots that alone allow already the distinction between K in  and K out  channels. Among them is a loop between TMD S5 and the pore that is very short in animal K out , longer in plant and animal K in  and the longest in plant K out  channels. In combination with further structural and phylogenetic analyses this finding suggests that outward-rectification evolved twice and independently in the animal and plant kingdom.

Outward Rectification of Voltage-Gated K+ Channels Evolved at Least Twice in Life History