IndraLab

Statements

PKC phosphorylates KCNC4. 5 / 5
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sparser
"Here, we focus on Kv3.4 NTID phosphorylation by PKC, with emphasis on the structural, biophysical and physiological impacts of this modification."
40288604
sparser
"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."
9649584
sparser
"However, other pathways in the spinal cord, such as descending inhibition involving serotonin ( xref ), may also contribute to PKC-dependent phosphorylation of presynaptic Kv3.4."
39739796
rlimsp
"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."
9649584
sparser
"For instance, protein kinase C phosphorylation of multiple serine residues in the Kv3.4 N-terminus dramatically attenuates the N-type inactivation normally observed in this channel ( Beck et al., 1998[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
16316679