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Article

Sites of the NUDT9-H domain critical for ADP-ribose activation of the cation channel TRPM2.

The Journal of biological chemistry - 5 Nov 2004

Kühn Frank J P, Lückhoff Andreas

Abstract excerpt

TRPM2 is a cation channel unique within the transient receptor potential family because of its gating by ADP-ribose (ADPR). ADPR gating is enabled by a cytosolic C-terminal Nudix box sequence motif embedded into a region homologous to the NUDT9 ADPR pyrophosphatase. A recently discovered splice variant of TRPM2 (TRPM2-DeltaC) lacks 34 amino acid residues in the NUDT9 domain and is insensitive to ADPR. To analyze...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 15347676
DOI: 10.1074/jbc.M407263200

Genes

TRPM2
NUDT9

Provenance

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.

Related research

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Sites of the NUDT9-H domain critical for ADP-ribose activation of the cation channel TRPM2.PMID 15347676Read ↗

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Analysis of ligand binding and resulting conformational changes in pyrophosphatase NUDT9.Semantic proximity Read ↗

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