IndraLab

Statements

STX1A binds KCNQ2. 16 / 16
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"The selective interaction of syntaxin 1A with KCNQ2, combined with a numerical simulation of syntaxin 1A's impact in a firing-neuron model, suggest that syntaxin 1A's interaction is targeted at regulating KCNQ2 channels to fine-tune presynaptic transmitter release, without interfering with the function of KCNQ2/3 channels in neuronal firing frequency adaptation."
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sparser
"First, we carried out a comparative examination of the physical interactions of syntaxin 1A with the channels by performing reciprocal coimmunoprecipitation analysis, using antibodies against KCNQ2, KCNQ3 and syntaxin 1A, in oocytes from a single batch coexpressing the subunits with syntaxin 1A. Syntaxin 1A associated with KCNQ2, to a lesser extent with KCNQ2/3 and only weakly with KCNQ3 ( xref )."
19675672
sparser
"Quantification over several similar experiments of the intensity ratios of coprecipitated syntaxin 1A to the different channel subunits, coexpressed in the same cells, showed that the amount of syntaxin 1A associated with KCNQ2 was ∼two-, five- and threefold larger than that with KCNQ2/3, KCNQ3 and KCNQ1, respectively ( xref )."
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sparser
"The interaction of syntaxin 1A with KCNQ2 prolonged the activation time constants of this conductance and reduced the conductance of the current roughly twofold ( xref )."
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"Syntaxin 1A strongly associates with KCNQ2 subunits but not with other KCNQ family members in Xenopus oocytes."
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"Pull-down and coimmunoprecipitation analyses in hippocampal and cortical synaptosomes demonstrated a physical interaction of brain KCNQ2 with syntaxin 1A, and confocal immunofluorescence microscopy showed high colocalization of KCNQ2 and syntaxin 1A at presynaptic varicosities."
19675672
sparser
"The strong in-vitro binding of syntaxin 1A ( xref ) and the inability of syntaxin 1A to associate with KCNQ2 lacking helix A in oocytes ( xref ), gave support to the notion that helix A is a crucial region for KCNQ2-syntaxin 1A binding."
19675672
sparser
"We further aimed to establish the role of helix A in the KCNQ2-syntaxin 1A interaction in oocytes by performing a coimmunoprecipitation analysis with two KCNQ2 deletion mutants, one lacking helix A itself (L339-W360) and the second lacking a dispensable stretch that separates helix A from helix B (L372-W493), which served as a control."
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sparser
"In the present study, we demonstrate that syntaxin 1A also associates with KCNQ2 subunits in the brain, leading to modulation of KCNQ2 homomeric channel gating in oocytes."
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"Follow-up experiments to further evaluate the interaction between syntaxin 1A and KCNQ2 at presynaptic terminals were carried out using two different assays in rat cortical and hippocampal synaptosomes."
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"We concluded that the in-vitro binding of syntaxin 1A to KCNQ2 is targeted to a defined region, strong, dose-dependent and saturable."
19675672
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"Since our results suggested a strong interaction between syntaxin 1A and KCNQ2 subunits, we checked whether the two proteins colocalize in dissociated cultures of hippocampal neurons."
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sparser
"These channels are known to be modulated by syntaxin-1A (Syn-1A) that binds to the C-terminal domain of the Kv7.2 subunit and strongly inhibits M current."
29067685
sparser
"Syntaxin 1A bound strongly to KCNQ2 and Δ372–493 deletion mutant, but did not bind Δ339–360 deletion mutant at all and therefore xref clearly shows that helix A is crucial for the binding."
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sparser
"KCNQ2 associates with syntaxin 1A in cortical and hippocampal synaptosomes."
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sparser
"Syntaxin-1A can bind to the C-terminus of Kv7.2 subunit, thereby decreasing open probability via facilitation of the interaction between the C-terminus and the N-terminus ( xref )."
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