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ERK phosphorylates KCND2. 35 / 35
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"Complementary to these pharmacological results, biochemical studies reveal that Kv4.2 was phosphorylated by ERK [ xref , xref ]."
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"ERK1/2 phosphorylates and inactivates the potassium channel subunit Kv4.2 (Adams et al., 2000), and by that mechanism may reduce A-current and thereby alter the excitability of presympathetic PVN neurons (Sonner and Stern, 2007)."
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"A-type potassium channels play a pivotal role in modulating neuron excitability; in fact, their downregulation may increase pain sensation. xref The A-type potassium channel Kv4.2 has been detected in DRG neurons and appears to be responsible for the transient A-type potassium current ( I A ) recorded in small DRG neurons. xref Kv4.2 is a known substrate for ERK1/2. xref The phosphorylation of Kv4.2 by ERK1/2 in dorsal horn neurons underlies the induction of central sensitisation and is critical for pain modulation. xref "
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"Kv4.2 phosphorylation by ERK results in inhibition of Kv4.2, leading to increase of dendritic excitability and enhanced LTP induction (Hoffman et al., 1997; Johnston et al., 2000, Chen et al., 2006; Schrader et al., 2006)."
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"Moreover, selective activation of extrasynaptic NMDA receptors decreases phosphorylation of Kv4.2 at ERK sites."
19850106
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"Importantly, a signalling pathway involving metabotropic glutamate receptor activation and extracellular signal-regulated kinase dependent phosphorylation of Kv4.2 channels has been shown to regulate I Ar currents in SDH neurons [ xref , xref ]."
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"Another study by Xu et al. also found that sodium butyrate enema induced VH by increased DRG neuronal excitability via activation of MAPK–ERK1/2, which phosphorylates Kv4.2, leading to a reduction in transient potassium current ( xref )."
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"In particular, ERK-dependent phosphorylation of the Kv4.2 potassium channel subunit has been shown to reduce A-type currents and increase excitability of CA1 pyramidal neurons, an effect that could be[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"There are three S/T-P sites at the C-terminus of Kv4.2 that can be phosphorylated by extracellular signal–regulated kinases (ERKs) xref ."
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"For example, the stratum lacunosum moleculare, which receives inputs from the entorhinal cortex via the perforant pathway, displays relatively little ERK-phosphorylated Kv4.2 or PKA carboxy-terminal-phosphorylated Kv4.2."
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"Consistent with previously published studies, elevating synaptic activity is associated with an increase in phosphorylation of Kv4.2 at ERK sites."
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"The phosphorylation of Kv4.2 by ERK1/2 in dorsal horn neurons underlies the induction of central sensitisation and is critical for pain modulation."
22833396
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"In addition, there is substantial evidence supporting the role of kinase regulation of A-type potassium currents in neurons, demonstrating a direct phosphorylation of the Kv4.2 channel subunit by PKA [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In particular, ERK-dependent phosphorylation of the Kv4.2 potassium channel subunit has been shown to reduce A-type currents and increase excitability of CA1 pyramidal neurons, an effect that could be[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"ERK1/2 phosphorylates and inactivates the potassium channel subunit Kv4.2 ( xref ), and by that mechanism may reduce A-current and thereby alter the excitability of presympathetic PVN neurons ( xref )."
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"Thus, visceral hypersensitivity induced by colonic NaB treatment appears to be mediated by activation of ERK1/2, which phosphorylates the Kv4.2 channel, resulting in a reduction in I and an enhancement of DRG neuronal excitability."
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"Phosphospecific antibodies specific for Kv4.2 phosphorylated at S552 revealed no obvious changes in phosphorylation in response to status epilepticus , in animal subjects where changes in Erk phosphorylation of Kv4.2 were observed [ xref ]."
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"In conclusion, our studies showed that increased DRG neuronal excitability is mediated by activation of MAPK–ERK1/2, which phosphorylates Kv4.2, leading to a reduction in I ."
22833396
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"Subsequently, phosphorylation of Kv4.2 by ERK1/2 resulted in a decrease in the number of channels on the cell surface, leading to dynamic down-regulation of channel function."
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"Kv4.2 is directly phosphorylated by ERK at three sites (Thr602, Thr607, and Ser616) [ xref ]."
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"Subsequently, phosphorylation of Kv4.2 by ERK1/2 resulted in a decrease in the number of channels on the cell surface, leading to dynamic down-regulation of channel function."
26456351
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"Phosphorylation of Kv4.2 by ERK at this site has been shown to inhibit opening of the channel, resulting in less hyperpolarization and a net increase in neuronal firing rate, as shown by increased exc[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"ERK regulates dendritic A-type K currents via direct phosphorylation of the Kv4.2 potassium channels."
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"The potential phosphorylation sites for PKC and for casein kinase II present in the intracellular domains of DPPX-K, -S, and -L (figure legend of Fig. 1 ) could add levels of modulation of A-type cha[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"These results indicate that PACAP/PAC1 signaling in hippocampal neurons could lead to dynamic phosphorylation of Kv4.2 protein, and PKA/ERK-dependent internalization of the channel protein from the cell surface."
26456351
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"We next investigated the role of ERK1/2 phosphorylation of Kv4.2 in the PACAP-induced reduction in channel function/density."
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"We next investigated the role of ERK1/2 phosphorylation of Kv4.2 in the PACAP-induced reduction in channel function/density."
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"Of the 3 amino acid residues in Kv4.2 that can be phosphorylated by ERK1/2, we found that the Kv4.2-T602A mutant exhibited a significant PACAP38-mediated decrease in channel current density, to an extent similar to that observed in WT channels ( xref )."
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"Altogether, these results suggest that PACAP38-mediated activation of PKA and PKC converges on ERK1/2 activation, which subsequently leads to phosphorylation of Kv4.2."
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"Importantly, a signalling pathway involving metabotropic glutamate receptor activation and extracellular signal-regulated kinase dependent phosphorylation of Kv4.2 channels has been shown to regulate I currents in SDH neurons [44,45]."
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"Phosphorylation of Kv4.2 by ERK at this site has been shown to inhibit opening of the channel, resulting in less hyperpolarization and a net increase in neuronal firing rate, as shown by increased exc[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"For example, Schrader et al. [23] reported that direct phosphorylation of Kv4.2 by ERK/MAPK caused a decrease in the Kv4.2-mediated outward K + current."
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"Moreover, kinase regulation may involve accessory proteins such as KChIP, as has been shown for neuronal Kv4.2 channels phosphorylated by ERK [48] ."
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"We determined that this antibody recognizes ERK-phosphorylated Kv4.2 in COS-7 cells transfected with Kv4.2 and native ERK-phosphorylated Kv4.2 in the rat hippocampus."
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"HFE increased phosphorylation of the Kv4.2 potassium channel, extracellular signal-regulated kinase, and cAMP response element-binding protein, which were reduced in the hippocampus of SPS+FS mice."
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