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Article

The 5-hydroxytryptamine(1A) receptor is stably palmitoylated, and acylation is critical for communication of receptor with Gi protein.

The Journal of biological chemistry - 30 Jan 2004

Papoucheva Ekaterina, Dumuis Aline, Sebben Michèle, Richter Diethelm W, Ponimaskin Evgeni G

Abstract excerpt

In the present study, we verified that the mouse 5-hydroxytryptamine(1A) (5-HT(1A)) receptor is modified by palmitic acid, which is covalently attached to the protein through a thioester-type bond. Palmitoylation efficiency was not modulated by receptor stimulation with agonists. Block of protein synthesis by cycloheximide resulted in a significant reduction of receptor acylation, suggesting that palmitoylation...

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Share to GTP-Binding Protein alpha Subunits, Gi-Go

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Identifiers

PMID: 14604995
DOI: 10.1074/jbc.M308177200

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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.

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The 5-hydroxytryptamine(1A) receptor is stably palmitoylated, and acylation is critical for communication of receptor with Gi protein.PMID 14604995Read ↗

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