ArticleThe Journal of biological chemistry2008
N-glycan-mediated quality control in the endoplasmic reticulum is required for the expression of correctly folded delta-opioid receptors at the cell surface.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 57 citations in OpenAlex.
- Delta Opioid Receptors within the Cortico-Thalamic Circuitry Underlie Hyperactivity Induced by High-Dose Morphine.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Functional Divergence for N-Linked Glycosylation Sites in Equine Lutropin/Choriogonadotropin Receptors.Current issues in molecular biology · 2025Article
- One immune system plays many parts: The dynamic role of the immune system in chronic pain and opioid pharmacology.Neuropharmacology · 2023Review
- Functional expression of opioid receptors and other human GPCRs in yeast engineered to produce human sterols.Nature communications · 2022Article
- Metabolomics reveals biomarkers of opioid use disorder.Translational psychiatry · 2021Article
- Post-Translational Modifications of G Protein-Coupled Receptors Control Cellular Signaling Dynamics in Space and Time.Pharmacological reviews · 2021Review
- Post-translational Modifications of Opioid Receptors.Trends in neurosciences · 2020Review
- N-glycosylation of αScientific reports · 2020Article
- G Protein-Coupled Receptors in the Sweet Spot: Glycosylation and other Post-translational Modifications.ACS pharmacology & translational science · 2020Review
- A forward genetic screen identifies chaperone CNX-1 as a conserved biogenesis regulator ofThe Journal of general physiology · 2018Article
- Site-specificThe Journal of biological chemistry · 2017Article
- Molecular Pharmacology of δ-Opioid Receptors.Pharmacological reviews · 2016Review
- Identification of Glycosylation Sites Essential for Surface Expression of the CaVα2δ1 Subunit and Modulation of the Cardiac CaV1.2 Channel Activity.The Journal of biological chemistry · 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
- Chaperoning G protein-coupled receptors: from cell biology to therapeutics.Endocrine reviews · 2014Review
- Protein homeostasis at the plasma membrane.Physiology (Bethesda, Md.) · 2014Review
- N-Glycan-dependent and -independent quality control of human δ opioid receptor N-terminal variants.The Journal of biological chemistry · 2014Article
- Stabilization of the μ-opioid receptor by truncated single transmembrane splice variants through a chaperone-like action.The Journal of biological chemistry · 2013Article
- Minireview: the intimate link between calcium sensing receptor trafficking and signaling: implications for disorders of calcium homeostasis.Molecular endocrinology (Baltimore, Md.) · 2012Review
- Cys-27 variant of human δ-opioid receptor modulates maturation and cell surface delivery of Phe-27 variant via heteromerization.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A great majority of G protein-coupled receptors are modified by N-glycosylation, but the functional significance of this modification for receptor folding and intracellular transport has remained elusive. Here we studied these phenomena by mutating the two N-terminal N-glycosylation sites (Asn(18) and Asn(33)) of the human delta-opioid receptor, and expressing the mutants from the same chromosomal integration site in stably transfected inducible HEK293 cells. Both N-glycosylation sites were used, and their abolishment decreased the steady-state level of receptors at the cell surface. However, pulse-chase labeling, cell surface biotinylation, and immunofluorescence microscopy revealed that this was not because of intracellular accumulation. Instead, the non-N-glycosylated receptors were exported from the endoplasmic reticulum with enhanced kinetics. The results also revealed differences in the significance of the individual N-glycans, as the one attached to Asn(33) was found to be more important for endoplasmic reticulum retention of the receptor. The non-N-glycosylated receptors did not show gross functional impairment, but flow cytometry revealed that a fraction of them was incapable of ligand binding at the cell surface. In addition, the receptors that were devoid of N-glycans showed accelerated turnover and internalization and were targeted for lysosomal degradation. The results accentuate the importance of protein conformation-based screening before export from the endoplasmic reticulum, and demonstrate how the system is compromised when N-glycosylation is disrupted. We conclude that N-glycosylation of the delta-opioid receptor is needed to maintain the expression of fully functional and stable receptor molecules at the cell surface.
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