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Article

N-linked protein glycosylation is a major determinant for basal TRPC3 and TRPC6 channel activity.

The Journal of biological chemistry - 28 Nov 2003

Dietrich Alexander, Mederos y Schnitzler Michael, Emmel Jens, Kalwa Hermann, Hofmann Thomas, Gudermann Thomas

Abstract excerpt

The TRPC family of receptor-activated cation channels (TRPC channels) can be subdivided into four subfamilies based on sequence homology as well as functional similarities. Members of the TRPC3/6/7 subfamily share common biophysical characteristics and are activated by diacylglycerol in a membrane-delimited manner. At present, it is only poorly understood whether members of the TRPC3/6/7 subfamily are...

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Identifiers

PMID: 12970363
DOI: 10.1074/jbc.M302983200

Genes

TRPC3
TRPC6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

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N-linked protein glycosylation is a major determinant for basal TRPC3 and TRPC6 channel activity.PMID 12970363Read ↗

Constitutive Inhibition of Transient Receptor Potential Canonical Type 6 (TRPC6) by O-GlcNAcylation at Threonine-221Semantic proximity Read ↗

TRPC3: a multifunctional signaling molecule.Semantic proximity Read ↗

Post-Translational Modification and Natural Mutation of TRPC Channels.Semantic proximity Read ↗

A mutation in TRPC6 channels abolishes their activation by hypoosmotic stretch but does not affect activation by diacylglycerol or G protein signaling cascades.Semantic proximity Read ↗

Transient receptor potential canonical 7: a diacylglycerol-activated non-selective cation channel.Semantic proximity Read ↗

Effects of N-glycosylation on hyperpolarization-activated cyclic nucleotide-gated (HCN) channels.Semantic proximity Read ↗

Structure-function analyses of the ion channel TRPC3 reveal that its cytoplasmic domain allosterically modulates channel gating.Semantic proximity Read ↗

N-linked glycosylation sites determine HERG channel surface membrane expression.Semantic proximity Read ↗

N-glycosylation determines the abundance of the transient receptor potential channel TRPP2.Semantic proximity Read ↗

Membrane topology of NAADP-sensitive two-pore channels and their regulation by N-linked glycosylation.Semantic proximity Read ↗

Formation of novel TRPC channels by complex subunit interactions in embryonic brain.Semantic proximity Read ↗

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