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Kv7.2 LC-MSMS - Updating in vivo and in vitro phosphorylation and methylation sites of voltage-gated Kv7

ABSTRACT: Voltage-gated Kv7.2 potassium channels regulate neuronal excitability. The gating of Kv7 channels is regulated by various mediators and neurotransmitters acting via G protein-coupled receptors; the underlying signalling cascades involve phosphatidylinositol-4,5-bisphosphate (PIP2), Ca2+/Calmodulin and phosphorylation. Recent studies have reported that PIP2 sensitivity of Kv7.2 channels is affected by two PTMs, phosphorylation and methylation, harboured in the PIP2 binding domains. Here this project aimed to update phosphorylation and methylation sites on Kv7.2 from heterologous cells, the rat brain and GST-fusion Kv7.2 N- and C-terminal ends proteins.

INSTRUMENT(S): Bruker Daltonics micrOTOF series, Bruker Daltonics amaZon series

ORGANISM(S): Rattus Norvegicus (rat) Homo Sapiens (human)

TISSUE(S): Brain, Hek-293 Cell

SUBMITTER: Jae-Won Yang

LAB HEAD: Jae-Won Yang

PROVIDER: PXD005567 | Pride | 2017-08-25

REPOSITORIES: Pride

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Updating In Vivo and In Vitro Phosphorylation and Methylation Sites of Voltage-Gated Kv7.2 Potassium Channels.

Erdem Fatma Asli FA Salzer Isabella I Heo Seok S Chen Wei-Qiang WQ Jung Gangsoo G Lubec Gert G Boehm Stefan S Yang Jae-Won JW

Proteomics 20171001 19

Voltage-gated Kv7.2 potassium channels regulate neuronal excitability. The gating of these channels is tightly controlled by various mediators and neurotransmitters acting via G protein-coupled receptors; the underlying signaling cascades involve phosphatidylinositol-4,5-bisphosphate (PIP2 ), Ca2+ /calmodulin, and phosphorylation. Recent studies found that the PIP2 sensitivity of Kv7.2 channels is affected by two posttranslational modifications, phosphorylation a ...[more]

PMID: 28834300

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