ArticleThe Journal of biological chemistry2010
Amino acid residues critical for endoplasmic reticulum export and trafficking of platelet-activating factor receptor.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 28 citations in OpenAlex.
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- Staphylococcus aureus toxin LukSF dissociates from its membrane receptor target to enable renewed ligand sequestration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Biomolecular engineering for nanobio/bionanotechnology.Nano convergence · 2017Review
- A clickable neurosteroid photolabel reveals selective Golgi compartmentalization with preferential impact on proximal inhibition.Neuropharmacology · 2016Article
- The atypical N-glycosylation motif, Asn-Cys-Cys, in human GPR109A is required for normal cell surface expression and intracellular signaling.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- Regulation of α2B-Adrenerigc Receptor Export Trafficking by Specific Motifs.Progress in molecular biology and translational science · 2015Review
- Visualization of the pH-dependent dynamic distribution of G2A in living cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- Protein ligation in living cells using sortase.Traffic (Copenhagen, Denmark) · 2012Article
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9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several residues are conserved in the transmembrane domains (TMs) of G-protein coupled receptors. Here we demonstrate that a conserved proline, Pro(247), in TM6 of platelet-activating factor receptor (PAFR) is required for endoplasmic reticulum (ER) export and trafficking after agonist-induced internalization. Alanine-substituted mutants of the conserved residues of PAFRs, including P247A, were retained in the ER. Because a PAFR antagonist, Y-24180, acted as a pharmacological chaperone to rescue ER retention, this retention is due to misfolding of PAFR. Methylcarbamyl (mc)-PAF, a PAFR agonist, did not increase the cell surface expression of P247A, even though another ER-retained mutant, D63A, was effectively trafficked. Signaling and accumulation of the receptors in the early endosomes were observed in the mc-PAF-treated P247A-expressing cells, suggesting that P247A was trafficked to the cell surface by mc-PAF, and thereafter disappeared from the surface due to aberrant trafficking, e.g. enhanced internalization, deficiency in recycling, and/or accelerated degradation. The aberrant trafficking was confirmed with a sortase-A-mediated method for labeling cell surface proteins. These results demonstrate that the conserved proline in TM6 is crucial for intracellular trafficking of PAFR.
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