IndraLab

Statements


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sparser
"Using the interaction of VAMP2 with Kv2.1 in Xenopus oocytes as a probe, we showed that coexpression of the t-SNARE complex with VAMP2 abolished the VAMP2 effect on channel inactivation and reduced the amount of VAMP2 that coprecipitated with Kv2.1."

sparser
"Given the proposed role for surface VAMP2 in the regulation of the vesicle cycle and the important role for the sustained Kv2.1 current in the regulation of dendritic calcium entry during high-frequency stimulation, the interaction of VAMP2 with Kv2.1 N terminus may contribute, alongside with the interaction of syntaxin with Kv2.1 C terminus, to the activity dependence of DCV release."

sparser
"VAMP2 interacts with relatively few ion channel proteins. xref were the first to report the interaction between VAMP2 and Kv2.1."

sparser
"In contrast to that seen with t-SNAREs, the Kv2.1-VAMP2 interaction does not involve the C-terminus of Kv2.1."

sparser
"Moreover, Kv2.1-VAMP2 interaction plays a fundamental role in the release of hormones, neuropeptides, and neurotrophic factors from DCVs ( xref ; xref )."

reach
"Lvov et al. (2008) were the first to report the interaction between VAMP2 and Kv2.1."

sparser
"It should be noted that in a different set of experiments, some VAMP2 binding to Kv2.1 C1a peptide was observed; its intensity was always significantly lower than that of syntaxin (not shown)."

sparser
"Recently, we showed that also VAMP2, the vesicular SNARE, interacts physically and functionally with Kv2.1."

sparser
"We report here that Kv2.1 interacts with VAMP2, the vesicular SNARE partner that is also present at high concentration in neuronal plasma membrane."