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Updated: Aug 19, 2026

Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels
Published on: May 18, 2009
Characterization of voltage-dependent gating of P2X2 receptor/channel
1Cellular and Molecular Pharmacology Section, Division of Pharmacology, National Institute of Health Sciences, 1-18-1 Kamiyoga, Setagaya, Tokyo 158-8501, Japan. nakazawa@nihs.go.jp
Abstract:
The role of a voltage-dependent gate of recombinant P2X2 receptor/channel was investigated in Xenopus oocytes. When a voltage step to -110 mV was applied from a holding potential of -50 mV, a gradual increase was observed in current evoked by 30 microM ATP. Contribution of this voltage-dependent component to total ATP-evoked current was greater when the current was evoked by lower concentrations of ATP. The voltage-dependent gate closed upon depolarization, and half the gates were closed at -80 mV. On the other hand, a potential at which half the gates opened was about -30 mV or more positive, which was determined using a series of hyperpolarization steps. The results of the present study suggest that the voltage-dependent gate behavior of P2X2 receptor is not due to simple activation and deactivation of a single gate, but rather due to transition from a low to a high ATP affinity state.
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