IndraLab

Statements


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sparser
"Indeed, this is true in both rodent and human β-cells, in which we demonstrated that disruption of the Kv2.1syntaxin 1A interaction impairs depolarization-induced exocytosis and insulin secretion ( xref )."

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sparser
"Syntaxin 1A alone binds strongly to Kv2.1 and shifts both activation and inactivation to hyperpolarized potentials."

sparser
"Kv2.1 interacts directly with syntaxin 1A, a plasma membrane t-SNARE component of the vesicle docking and fusion apparatus."

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sparser
"Here we demonstrate, using co-immunoprecipitation and immunocytochemistry analyses, the existence of a physical interaction in neuroendocrine cells between Kv2.1 and syntaxin 1A. Furthermore, using concomitant co-immunoprecipitation from plasma membranes and two-electrode voltage clamp analyses in Xenopus oocytes combined with in vitro binding analysis, we characterized the effects of these interactions on the Kv2.1 channel gating pertaining to the assembly/disassembly of the syntaxin 1A/SNAP-25 (target (t)-SNARE) complex."

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sparser
"This phenomenon relies on Kv2.1 binding to syntaxin 1A via 9 amino acids within the channel intrinsically disordered C terminus."

sparser
"Colocalization of KCNQ2 and syntaxin 1A at synaptic terminals suggests a role for their interaction in vesicle release, similar to the recently identified novel role for the syntaxin 1A-Kv2.1 interaction in the enhancement of dense-core vesicle release xref , xref ."

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