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Comparative sequence analysis suggests a conserved gating mechanism for TRP channels.

Eugene Palovcak1, Lucie Delemotte1, Michael L Klein1

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|June 17, 2015
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Transient receptor potential (TRP) channels are polymodal sensors. Comparative analysis reveals TRP channel gating mechanisms differ from voltage-gated potassium (Kv) channels, involving an H-bond network in S6.

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Area of Science:

  • Molecular Biology
  • Biophysics
  • Cellular Physiology

Background:

  • Transient receptor potential (TRP) channels are crucial for sensory transduction in eukaryotes.
  • TRP channels, despite sequence diversity, form tetrameric structures akin to voltage-gated potassium (Kv) channels.
  • Understanding the gating mechanisms of TRP channels is essential for elucidating sensory perception.

Purpose of the Study:

  • To investigate if the allosteric gating mechanism is conserved across all TRP channels.
  • To compare the TRP channel gating mechanism with that of Kv channels.
  • To propose a novel model for TRP channel gating.

Main Methods:

  • Comparative sequence analysis of extensive TRP and Kv channel datasets.
  • Identification of conserved and correlated sequence patterns.
  • Integration of insights from recent TRPV1 structures.

Main Results:

  • Identification of sequence features unique to TRP channels.
  • TRP channel gating mechanism differs significantly from Kv channel voltage sensitivity.
  • A proposed model for TRP channel gating involving an S6 H-bond network defect.

Conclusions:

  • The allosteric gating mechanism in TRP channels is polymodal and distinct from Kv channel voltage gating.
  • TRP channel gating involves specific sequence features and an S6 H-bond network.
  • This study provides a new framework for understanding TRP channel function.