"We found that pkc specifically eliminates rapid inactivation of a cloned human a-type k+ channel (hkv3.4), converting this channel from a rapidly inactivating a type to a noninactivating delayed rectifier type."
"This study investigated the molecular physiology of the nh2-terminal phosphorylation sites that regulate inactivation gating of an a-type k+ channel. The main results show that: (a) pkc acts on four phosphate acceptors (s8, s9, s15, and s21) within the inactivation domain because mutation of these residues to alanine is necessary and sufficient to remove the action of pkc on channel inactivation."
"This study investigated the molecular physiology of the nh2-terminal phosphorylation sites that regulate inactivation gating of an a-type k+ channel. The main results show that: (a) pkc acts on four phosphate acceptors (s8, s9, s15, and s21) within the inactivation domain because mutation of these residues to alanine is necessary and sufficient to remove the action of pkc on channel inactivation."
"We found that pkc specifically eliminates rapid inactivation of a cloned human a-type k+ channel (hkv3.4), converting this channel from a rapidly inactivating a type to a noninactivating delayed rectifier type."
"We found that pkc specifically eliminates rapid inactivation of a cloned human a-type k+ channel (hkv3.4), converting this channel from a rapidly inactivating a type to a noninactivating delayed rectifier type."
"This study investigated the molecular physiology of the nh2-terminal phosphorylation sites that regulate inactivation gating of an a-type k+ channel. The main results show that: (a) pkc acts on four phosphate acceptors (s8, s9, s15, and s21) within the inactivation domain because mutation of these residues to alanine is necessary and sufficient to remove the action of pkc on channel inactivation."
"We found that pkc specifically eliminates rapid inactivation of a cloned human a-type k+ channel (hkv3.4), converting this channel from a rapidly inactivating a type to a noninactivating delayed rectifier type."
"This study investigated the molecular physiology of the nh2-terminal phosphorylation sites that regulate inactivation gating of an a-type k+ channel. The main results show that: (a) pkc acts on four phosphate acceptors (s8, s9, s15, and s21) within the inactivation domain because mutation of these residues to alanine is necessary and sufficient to remove the action of pkc on channel inactivation."
"These results confirmed that the NH 2 -terminal inactivation domain of Kv3.4 is phosphorylated by PKC and that this modification is associated with elimination of N-type inactivation by PKC in the intact channel."
"These results confirmed that the NH2-terminal inactivation domain of Kv3.4 is phosphorylated by PKC and that this modification is associated with elimination of N-type inactivation by PKC in the intact channel."
"To explain how phosphorylation of a set of four serines at positions 8, 9, 15, and 21 by PKC causes elimination of rapid N-type inactivation in Kv3.4, we have considered two possible mechanisms."
"Kv3.4 channels help shape the repolarization of the nociceptor APs, and that modulation of Kv3.4 channel N-type inactivation by PKC regulates AP repolarization and duration suggesting that the dramatic modulation of high voltage-activated A-type K+ current ( I A HV ) fast inactivation by PKC represents a novel mechanism of neural plasticity with potentially significant implications in the transition from acute to chronic pain [ xref ]."
"These results show that Kv3.4 channels help shape the repolarization of the nociceptor AP, and that modulation of Kv3.4 channel N-type inactivation by PKC regulates AP repolarization and duration."
"In expression systems, the channels produced by the expression of Kcnc1 and Kcnc2 produce delayed rectifier K + currents, whereas the expression of Kcnc3 and Kcnc4 produce inactivating A-type K + currents."