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The movement of ions like sodium, potassium, and calcium into and out of the cell is essential to maintain the electrochemical gradient in living cells. The ion channels—a class of membrane transport proteins—help maintain this ionic gradient for the smooth functioning of physiological activities such as maintaining cell size and volume, conducting nerve impulses, and gas and nutrient exchange.
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This article presents a method for real-time, quantitative monitoring of calcium ion (Ca2+) concentrations in cells using single-cell Ca2+ imaging with the Fura-2/AM dye. This technique enables efficient dye loading and accurate calculation of Ca2+ levels through fluorescence intensity ratios, making it a simple and rapid approach for research...
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Related Experiment Video

Updated: Jan 20, 2026

Ligand Gated and Voltage Gated Ion Channels
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Recent progress in structural studies on canonical TRP ion channels.

Wenjun Guo1, Lei Chen2

  • 1State Key Laboratory of Membrane Biology, Institute of Molecular Medicine, Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Beijing 100871, China.

Cell Calcium
|September 7, 2019
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Summary

Canonical transient receptor potential (TRPC) channels are crucial for physiological functions. Structural analysis reveals conserved architectures and subtype-specific features across the TRPC family, highlighting key differences in their domains.

Keywords:
BTDMIon channelTRPTRPC

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Structural Biology

Background:

  • Canonical transient receptor potential (TRPC) channels are essential non-selective cation channels involved in diverse physiological processes.
  • Understanding TRPC channel structure is key to elucidating their function in cellular signaling.
  • Previous studies have provided structural insights into various TRPC subtypes.

Purpose of the Study:

  • To review and analyze the structural differences among various TRPC channel subtypes.
  • To highlight conserved architectural features and unique characteristics of TRPC proteins.
  • To focus on variations in extracellular, transmembrane, and cytoplasmic domains.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) structure determination.
  • Comparative structural analysis of resolved TRPC channel subtypes.
  • Bioinformatic analysis of structural data.

Main Results:

  • Cryo-EM structures of TRPC channels range from 2.8 Å to 5.8 Å resolution.
  • Conserved architectural frameworks are evident across the TRPC family.
  • Distinct structural variations are identified in extracellular, transmembrane, and cytoplasmic regions specific to TRPC subtypes.

Conclusions:

  • TRPC channel structures exhibit both conserved elements and subtype-specific variations.
  • Detailed structural comparisons provide a foundation for understanding TRPC channel function and regulation.
  • Further structural studies will refine our understanding of TRPC channel diversity.