ArticleMolecular pharmacology2009
Anterograde trafficking of G protein-coupled receptors: function of the C-terminal F(X)6LL motif in export from the endoplasmic reticulum.
Article in Molecular pharmacology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 69 citations in OpenAlex.
- Folding, misfolding, and regulation of intracellular traffic of G protein-coupled receptors involved in the hypothalamic-pituitary-gonadal axis.Andrology · 2026Review
- The ufmylation cascade controls COPII recruitment, anterograde transport, and sorting of nascent GPCRs at ER.Science advances · 2024Article
- Article
- Human C1orf27 protein interacts with αThe Journal of biological chemistry · 2022Article
- Specific motifs mediate post-synaptic and surface transport of G protein-coupled receptors.iScience · 2022Article
- Targeting trafficking as a therapeutic avenue for misfolded GPCRs leading to endocrine diseases.Frontiers in endocrinology · 2022Review
- Article
- Conserved C-terminal motifs in odorant receptors instruct their cell surface expression and cAMP signaling.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021Article
- Quantification of The Surface Expression of G Protein-coupled Receptors Using Intact Live-cell Radioligand Binding Assays.Bio-protocol · 2020Article
- A Naturally Occurring Splice Variant of GGA1 Inhibits the Anterograde Post-Golgi Traffic of αScientific reports · 2019Article
- Mechanisms of the anterograde trafficking of GPCRs: Regulation of AT1R transport by interacting proteins and motifs.Traffic (Copenhagen, Denmark) · 2019Review
- BetaBiochimica et biophysica acta. Biomembranes · 2017Article
- Olfactory Receptors in Non-Chemosensory Organs: The Nervous System in Health and Disease.Frontiers in aging neuroscience · 2016Review
- A single mutation in helix 8 enhances the angiotensin II type 1a receptor transport and signaling.Cellular signalling · 2015Article
- Regulation of α2B-Adrenerigc Receptor Export Trafficking by Specific Motifs.Progress in molecular biology and translational science · 2015Review
- Regulation of β-adrenergic receptor trafficking and lung microvascular endothelial cell permeability by Rab5 GTPase.International journal of biological sciences · 2015Article
- Golgi complex-plasma membrane trafficking directed by an autonomous, tribasic Golgi export signal.Molecular biology of the cell · 2014Article
- A membrane-proximal, C-terminal α-helix is required for plasma membrane localization and function of the G Protein-coupled receptor (GPCR) TGR5.The Journal of biological chemistry · 2014Article
- Recruitment of a cytoplasmic chaperone relay by the A2A adenosine receptor.The Journal of biological chemistry · 2013Article
- The angiotensin II type 1 receptor C-terminal Lys residues interact with tubulin and modulate receptor export trafficking.PloS one · 2013Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
We have reported previously that the F(X)(6)LL motif in the C termini is essential for export of alpha(2B)-adrenergic (alpha(2B)-AR) and angiotensin II type 1 receptors (AT1Rs) from the endoplasmic reticulum (ER). Here, we further demonstrate that mutation of the F(X)(6)LL motif similarly abolished the cell-surface expression of alpha(2B)-AR, AT1R, alpha(1B)-AR, and beta(2)-AR, suggesting that the F(X)(6)LL motif plays a general role in ER export of G protein-coupled receptors (GPCRs). Mutation of Phe to Val, Leu, Trp, and Tyr, and mutation of LL to FF and VV, markedly inhibited alpha(2B)-AR transport, indicating that the F(X)(6)LL function cannot be fully substituted by other hydrophobic residues. The structural analysis revealed that the Phe residue in the F(X)(6)LL motif is buried in the transmembrane domains and possibly interacts with Ile58 in beta(2)-AR and Val42 in alpha(2B)-AR, whereas the LL motif is exposed to the cytosolic space. Indeed, mutation of Ile58 in beta(2)-AR and Val42 in alpha(2B)-AR markedly disrupted cell surface transport of the receptors. It is noteworthy that the Val and Ile residues are highly conserved among the GPCRs carrying the F(X)(6)LL motif. Furthermore, the Phe mutant exhibited a stronger interaction with ER chaperones and was more potently rescued by physical and chemical treatments than the LL mutant. These data suggest that the Phe residue is probably involved in folding of alpha(2B)-AR and beta(2)-AR, possibly through interaction with other hydrophobic residues in neighboring domains. These data also provide the first evidence implying crucial roles of the C termini possibly through modulating multiple events in anterograde trafficking of GPCRs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.