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Article

TRPM8 voltage sensor mutants reveal a mechanism for integrating thermal and chemical stimuli.

Nature chemical biology - 1 Mar 2007

Voets Thomas, Owsianik Grzegorz, Janssens Annelies, Talavera Karel, Nilius Bernd

Abstract excerpt

TRPM8, a member of the transient receptor potential (TRP) channel superfamily, is expressed in thermosensitive neurons, in which it functions as a cold and menthol sensor. TRPM8 and most other temperature-sensitive TRP channels (thermoTRPs) are voltage gated; temperature and ligands regulate channel opening by shifting the voltage dependence of activation. The mechanisms and structures underlying gating of...

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Source

Identifiers

PMID: 17293875
DOI: 10.1038/nchembio862

Genes

TRPM8

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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TRPM8 voltage sensor mutants reveal a mechanism for integrating thermal and chemical stimuli.PMID 17293875Read ↗

Mutations of TRPM8 channels: Unraveling the molecular basis of activation by cold and ligands.Semantic proximity Read ↗

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Surface expression and channel function of TRPM8 are cooperatively controlled by transmembrane segments S3 and S4.Semantic proximity Read ↗

TRPV1 temperature activation is specifically sensitive to strong decreases in amino acid hydrophobicity.Semantic proximity Read ↗

Critical role of the pore domain in the cold response of TRPM8 channels identified by ortholog functional comparison.Semantic proximity Read ↗

Conserved residues within the putative S4-S5 region serve distinct functions among thermosensitive vanilloid transient receptor potential (TRPV) channels.Semantic proximity Read ↗

Ligand stoichiometry of the cold- and menthol-activated channel TRPM8.Semantic proximity Read ↗

The region adjacent to the C-end of the inner gate in transient receptor potential melastatin 8 (TRPM8) channels plays a central role in allosteric channel activation.Semantic proximity Read ↗

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