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Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints.
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KCNE5 (show KCNE1L Antibodies) subunits may affect Kv2.1 (show KCNB1 Antibodies) homotetramers and Kv2.1 (show KCNB1 Antibodies)/Kv6.4 heterotetramers in vivo, resulting in more tissue-specific fine-tuning mechanisms.
KvS subunits modify the pharmacological response of Kv2 (show KCNA6 Antibodies) subunits when assembled in heterotetramers and illustrate the potential of KvS subunits to provide unique properties to the heterotetramers, as is the case for 4-AP on Kv2.1 (show KCNB1 Antibodies)/Kv6.4 channels.
Obligatory heterotetramerization of three previously uncharacterized Kv channel subunits identified in human genome (Kv6.3)(Kv10.1 (show KCNG3 Antibodies)) (Kv11.1 (show KCNH2 Antibodies))
This study suggests that the silent behaviour of Kv6.3 is largely caused by the C-terminal part of its sixth transmembrane domain that causes ER retention of the subunit.
Mutation of histidine 105 in the T1 domain of the potassium channel Kv2.1 (show KCNB1 Antibodies) disrupts heteromerization with Kv6.3 and Kv6.4.
Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. This gene encodes a member of the potassium channel, voltage-gated, subfamily G. This member functions as a modulatory subunit. The gene has strong expression in brain. Multiple alternatively spliced variants have been found in normal and cancerous tissues.
potassium voltage-gated channel subfamily G member 4
, voltage-gated potassium channel Kv6.3
, voltage-gated potassium channel subunit Kv6.4
, voltage-gated potassium channel subunit Kv6.3