Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Role of the C-terminal di-leucine motif of 5-HT1A and 5-HT1B serotonin receptors in plasma membrane targeting.

Journal of cell science - 15 Oct 2006

Carrel Damien, Hamon Michel, Darmon Michèle

Abstract excerpt

The 5-HT1A and 5-HT1B serotonin receptors exhibit different subcellular localizations in neurons. Evidence has been reported that the C-terminal domain is involved in the somato-dendritic and axonal targeting of 5-HT1AR and 5-HT1BR, respectively. Here we analyzed the consequences of the mutation of a di-leucine motif and palmitoylated cysteines within this domain. Replacement of I414-I415 by a di-alanine in...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Chlorocebus aethiops
Share to Cysteine
Share to Endoplasmic Reticulum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescent Antibody Technique, Indirect

Share to Leucine

Share to Receptor, Serotonin, 5-HT1A

Share to Receptor, Serotonin, 5-HT1B

Share to Serotonin Receptor Agonists

Source

Identifiers

PMID: 17003106
DOI: 10.1242/jcs.03189

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

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of the C-terminal di-leucine motif of 5-HT1A and 5-HT1B serotonin receptors in plasma membrane targeting.PMID 17003106Read ↗

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

The recombinant 5-HT1A receptor: G protein coupling and signalling pathways.Semantic proximity Read ↗

Localization of the mouse 5-hydroxytryptamine(1A) receptor in lipid microdomains depends on its palmitoylation and is involved in receptor-mediated signaling.Semantic proximity Read ↗

Neuronal phenotype dependency of agonist-induced internalization of the 5-HT(1A) serotonin receptor.Semantic proximity Read ↗

Ligand recognition and G-protein coupling of trace amine receptor TAAR1.Semantic proximity Read ↗

Essential role of the C148-C227 disulphide bridge in the human 5-HT2A homodimeric receptor.Semantic proximity Read ↗

C-terminal di-leucine motif of dopamine D₁ receptor plays an important role in its plasma membrane trafficking.Semantic proximity Read ↗

Site-directed mutagenesis of the 5-HT1B receptor increases the affinity of 5-HT for the agonist low-affinity conformation and reduces the intrinsic activity of 5-HT.Semantic proximity Read ↗

Conversion of the human 5-HT1D beta serotonin receptor to the rat 5-HT1B ligand-binding phenotype by Thr355Asn site directed mutagenesis.Semantic proximity Read ↗

Identification of an amino acid residue important for binding of methiothepin and sumatriptan to the human 5-HT(1B) receptor.Semantic proximity Read ↗

The 5-hydroxytryptamine(4a) receptor is palmitoylated at two different sites, and acylation is critically involved in regulation of receptor constitutive activity.Semantic proximity Read ↗

Novel brain-specific 5-HT4 receptor splice variants show marked constitutive activity: role of the C-terminal intracellular domain.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.