ArticleThe Biochemical journal2005
Importance of N-glycosylation positioning for cell-surface expression, targeting, affinity and quality control of the human AT1 receptor.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 59 citations in OpenAlex.
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- Molecular Regulation of Lysophosphatidic Acid Receptor 1 Maturation and Desensitization.Cell biochemistry and biophysics · 2021Review
- Post-Translational Modifications of G Protein-Coupled Receptors Control Cellular Signaling Dynamics in Space and Time.Pharmacological reviews · 2021Review
- Thermostability of a recombinant G protein-coupled receptor expressed at high level in mammalian cell culture.Scientific reports · 2020Article
- Modulation of Endocannabinoid-Binding Receptors in Human Neuroblastoma Cells by Tunicamycin.Molecules (Basel, Switzerland) · 2019Article
- Discovery and functional characterisation of a luqin-type neuropeptide signalling system in a deuterostome.Scientific reports · 2018Article
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- Smoothened Regulation: A Tale of Two Signals.Trends in pharmacological sciences · 2016Review
- Functional Divergence in the Role of N-Linked Glycosylation in Smoothened Signaling.PLoS genetics · 2015Article
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- The membrane proteome of sensory cilia to the depth of olfactory receptors.Molecular & cellular proteomics : MCP · 2014Article
- Immunohistochemical detection of angiotensin II receptors in mouse cerebellum and adrenal gland using "in vivo cryotechnique".Histochemistry and cell biology · 2013Article
- Garlic (Allium sativum) down-regulates the expression of angiotensin II AT(1) receptor in adrenal and renal tissues of streptozotocin-induced diabetic rats.Inflammopharmacology · 2013Article
- Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.The Journal of biological chemistry · 2013Article
- Elucidation of relaxin-3 binding interactions in the extracellular loops of RXFP3.Frontiers in endocrinology · 2013Article
- Glycosylation of the sodium channel β4 subunit is developmentally regulated and involves in neuritic degeneration.International journal of biological sciences · 2012Article
- The role of N53Q mutation on the rat mu-opioid receptor function.Journal of biomolecular techniques : JBT · 2010Article
- Design, generation, and testing of mammalian expression modules that tag membrane proteins.Protein science : a publication of the Protein Society · 2009Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
GPCRs (G-protein-coupled receptors) are preferentially N-glycosylated on ECL2 (extracellular loop 2). We previously showed that N-glycosylation of ECL2 was crucial for cell-surface expression of the hAT1 receptor (human angiotensin II receptor subtype 1). Here, we ask whether positioning of the N-glycosylation sites within the various ECLs of the receptor is a vital determinant in the functional expression of hAT(1) receptor at the cell surface. Artificial N-glycosylation sequons (Asn-Xaa-Ser/Thr) were engineered into ECL1, ECL2 and ECL3. N-glycosylation of ECL1 caused a very significant decrease in affinity and cell surface expression of the resulting receptor. Shifting the position of the ECL2 glycosylation site by two residues led to the synthesis of a misfolded receptor which, nevertheless, was trafficked to the cell surface. The misfolded nature of this receptor is supported by an increased interaction with the chaperone HSP70 (heat-shock protein 70). Introduction of N-glycosylation motifs into ECL3 yielded mutant receptors with normal affinity, but low levels of cell surface expression caused by proteasomal degradation. This behaviour differed from that observed for the aglycosylated receptor, which accumulated in the endoplasmic reticulum. These results show how positioning of the N-glycosylation sites altered many properties of the AT1 receptor, such as targeting, folding, affinity, cell surface expression and quality control.
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