IndraLab

Statements


SRC phosphorylates KCNB1. 13 / 14
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sparser
"This result led us to evaluate whether NS5A1b could prevent Src phosphorylation of Kv2.1."

rlimsp
"The actions of the viral protein are genotype-selective, as NS5A1a does not depress neuronal potassium currents nor inhibit Src phosphorylation of Kv2.1."

sparser
"The actions of the viral protein are genotype-selective, as NS5A1a does not depress neuronal potassium currents nor inhibit Src phosphorylation of Kv2.1."

sparser
"NS5A1b modulates this process by interfering with the phosphorylation of Kv2.1 by Src."

sparser
"Additional studies revealed that the apoptotic potassium current surge results from a zinc-activated phosphorylation of Kv2.1 by both Src and p38, which in turn, induces a syntaxin-dependent de novo insertion of large number of Kv2.1 channels into the plasma membrane ( xref ; xref , xref ; xref )."

sparser
"However, a systematic analysis of the molecular mechanism of Kv2.1 channel phosphorylation by Src is lacking."

rlimsp
"Accordingly, NS5A1b coexpression prevents phosphorylation of wild-type Kv2.1 by Src at Y124, but is unable to inhibit p38 phosphorylation of the channel at S800."

sparser
"In previous studies [ xref , xref ], we reported that the phosphorylation of Kv2.1 by Src and p38 kinases is associated with oxidant-triggered apoptotic K + current surges in transfected CHO cells."

sparser
"This process is triggered by the phosphorylation of Kv2.1 by Src and p38 kinases at two distinct intracellular n- and c-terminal residues of the channel, Y124 and S800 ( xref , xref )."

sparser
"This may be a potential pathway involving CK2 which indirectly downregulates Src phosphorylation of Kv2.1 via PP2A activation, and thus diminishes Kv2.1 activity under normal, steady-state conditions."

sparser
"NS5A1b co-expression also inhibited this more modest Src-induced phosphorylation of Kv2.1(Y124F) (0.015 ± 0.004 r."

sparser
"Fortunately, most (~80%) of the Src phosphorylation of Kv2.1 occurs at this residue ( xref )."

sparser
"We identified two novel Tyr sites of Src-dependent phosphorylation in Kv2.1 channels and showed that mutation of these sites to non-phosphorylatable residues results in blockage or decrease of the K + current enhancement that is normally observed in the presence of active Src and that these sites regulate the activities and the surface expression levels of the channel when Src is present."