KV10.2 channels

Channel name KV10.2
Description Outward-rectifying, noninactivating voltage-dependent K+ currents3,4,5
Other names eag21,2,3,4,5
Molecular information Human: 987aa, NM_139318 (transcript variant 1), chr. 14q23.1, KCNH5 (see “Comments”), GeneID: 27133, PMID: 97384732
Mouse: 988aa, NM_172805, chr. 12
Rat: 988aa, NM_133610, chr. 6q24
Associated subunits Hyperkinetic (Hk),6 CaM, Slob, KCR1 (potassium channel regulator)
Functional assays Voltage-clamp
Current Outward-rectifying
Conductance Not established
Ion selectivity K+
Activation Activates at —100 mV (rat)3
Inactivation Noninactivating
Activators None
Gating inhibitors None
Blockers Quinidine (152 μM),5 intracellular calcium (nanomolar)4
Radioligands None
Channel distribution Brain (layer IV of the cerebral cortex; thalamus, inferior colliculus, olfactory bulb, and certain brainstem nuclei)3,4
Physiological functions Not established
Mutations and pathophysiology Not established
Pharmacological significance Not established
Comments This channel has a GFG (rather than the common GYG) potassium channel signature sequence, a PAS domain in the distal part of the cytosolic N terminus, a cNBD domain in the proximal portion of the C terminus, a C-terminal assembly domain (CAD), a CaM-binding domain, a bNLS domain in the C terminus, and a C-terminal domain is required for assembly7; the TCC domain at the C-terminal end of Kv10 and Kv11 confers specificity for multimer formation, allowing Kv10.1/Kv10.2 heteromerization and Kv11 homomerization but not Kv10.x/Kv11.x heteromerization8; this C-terminal TCC domain has been identified in many other channels, and mutations of the TCC have been found to be linked to genetic channelopathies
  • aa, amino acids; chr., chromosome; CaM, calmodulin; TCC, tetramerizing coiled-coiled.

  • 1. Shi W, Wang HS, Pan Z, Wymore RS, Cohen IS, McKinnon D, and Dixon JE (1998) Cloning of a mammalian elk potassium channel gene and EAG mRNA distribution in rat sympathetic ganglia. J Physiol 511:675-682

  • 2. Occhiodoro T, Bernheim L, Liu JH, Bijlenga P, Sinnreich M, Bader CR, and Fischer-Lougheed J (1998) Cloning of a human ether-à-go-go potassium channel expressed in myoblasts at the onset of fusion. FEBS Lett 434:177-182

  • 3. Saganich MJ, Vega-Saenz de Miera E, Nadal MS, Baker H, Coetzee WA, and Rudy B (1999) Cloning of components of a novel subthreshold-activating K+ channel with a unique pattern of expression in the cerebral cortex. J Neurosci 19:10789-10802

  • 4. Ludwig J, Weseloh R, Karschin C, Liu Q, Netzer R, Engeland B, Stansfeld C, and Pongs O (2000) Cloning and functional expression of rat eag2, a new member of the ether-à-go-go family of potassium channels and comparison of its distribution with that of eag1. Mol Cell Neurosci 16:59-70

  • 5. Schonherr R, Gessner G, Lober K, and Heinemann SH (2002) Functional distinction of human EAG1 and EAG2 potassium channels. FEBS Lett 514:204-208

  • 6. Wilson GF, Wang Z, Chouinard SW, Griffith LC, and Ganetzky B (1998) Interaction of the K channel β subunit, Hyperkinetic, with eag family members. J Biol Chem 273:6389-6394

  • 7. Ludwig J, Owen D, and Pongs O (1997) Carboxy-terminal domain mediates assembly of the voltage-gated rat ether-à-go-go potassium channel. EMBO J 16:6337-6345

  • 8. Jenke M, Sanchez A, Monje F, Stuhmer W, Weseloh RM, and Pardo LA (2003) C-terminal domains implicated in the functional surface expression of potassium channels. EMBO J 22:395-403