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Updated: Apr 29, 2026

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
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Extracellular disulfide bridges stabilize TRPC5 dimerization, trafficking, and activity.

Chansik Hong1, Misun Kwak, Jongyun Myeong

  • 1Department of Physiology and Institute of Dermatological Science, Seoul National University College of Medicine, 28 Yeongeon-dong, Jongno-gu, Seoul, 110-799, South Korea.

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Summary

A disulfide bond involving cysteine 553 in TRPC5 channels is crucial for their function. This bond regulates channel assembly, activity, and cell surface trafficking, impacting TRPC5 channel function.

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Area of Science:

  • Molecular biology
  • Biophysics
  • Cell biology

Background:

  • Cysteine residues and disulfide bonds are vital for protein structure and function.
  • Extracellular cysteine regulation in classical transient receptor potential (TRPC) channels is not fully understood.
  • TRPC5 channels play roles in various cellular processes, but their precise regulatory mechanisms require further investigation.

Purpose of the Study:

  • To investigate the functional significance of extracellular disulfide bonds in TRPC5 channels.
  • To determine the role of specific cysteine residues (C553 and C558) in TRPC5 channel gating and trafficking.
  • To elucidate the impact of disulfide bond formation on TRPC5 channel multimerization and activity.

Main Methods:

  • Utilized HEK293 cells transiently transfected with wild-type (WT) and mutant TRPC5 constructs (C553S, C558S).
  • Employed reducing agents to assess the role of disulfide bonds in channel formation and activity.
  • Measured TRPC5 channel currents using electrophysiology.
  • Investigated protein interactions using co-immunoprecipitation and Förster resonance energy transfer (FRET).
  • Analyzed channel trafficking and membrane distribution via cell surface expression studies.

Main Results:

  • A disulfide linkage was identified as essential for the tetrameric formation of TRPC5 channels.
  • Mutations in C553 or C558 abolished TRPC5 channel activity induced by lanthanides or receptor stimulation.
  • TRPC5 mutants exhibited dominant-negative effects, inhibiting WT TRPC5 channel activity.
  • Disulfide bond disruption reduced TRPC5 channel current and membrane localization.
  • Weakened dimeric interactions were observed between WT and mutant TRPC5 channels.

Conclusions:

  • The disulfide bond between conserved extracellular cysteines, particularly C553, is critical for functional TRPC5 channel activity.
  • This disulfide bond is essential for proper channel multimerization, gating, and trafficking to the plasma membrane.
  • Understanding this mechanism provides insights into TRPC channel regulation and potential therapeutic targets.