ArticleProceedings of the National Academy of Sciences of the United States of America2007
Functional consequences of alteration of N-linked glycosylation sites on the neurokinin 1 receptor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 64 citations in OpenAlex.
- The neuropeptide substance P regulates aldosterone secretion in human adrenals.Nature communications · 2020Trial
- Protein networking: nicotinic acetylcholine receptors and their protein-protein-associations.Molecular and cellular biochemistry · 2024Review
- Enrichment and fragmentation approaches for enhanced detection and characterization of endogenous glycosylated neuropeptides.Proteomics · 2023Article
- Comparative site-specific N-glycoproteome analysis reveals aberrant N-glycosylation and gives insights into mannose-6-phosphate pathway in cancer.Communications biology · 2023Article
- Functional Rescue of Inactivating Mutations of the Human Neurokinin 3 Receptor Using Pharmacological Chaperones.International journal of molecular sciences · 2022Article
- Mammalian Neuropeptides as Modulators of Microbial Infections: Their Dual Role in Defense versus Virulence and Pathogenesis.International journal of molecular sciences · 2021Review
- Post-Translational Modifications of G Protein-Coupled Receptors Control Cellular Signaling Dynamics in Space and Time.Pharmacological reviews · 2021Review
- Neurokinin receptors and their implications in various autoimmune diseases.Current research in immunology · 2021Review
- Time-Restricted G-Protein Signaling Pathways via GPR176, GInternational journal of molecular sciences · 2020Review
- Glycosylation and raft endocytosis in cancer.Cancer metastasis reviews · 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
- Identification and functional characterisation of N-linked glycosylation of the orphan G protein-coupled receptor Gpr176.Scientific reports · 2020Article
- RGS9-2 rescues dopamine D2 receptor levels and signaling inEMBO molecular medicine · 2019Article
- Investigation of the effect of homocysteinylation of substance P on its binding to the NK1 receptor using molecular dynamics simulation.Journal of molecular modeling · 2018Article
- MicroRNA-31-3p Is Involved in Substance P (SP)-Associated Inflammation in Human Colonic Epithelial Cells and Experimental Colitis.The American journal of pathology · 2018Article
- Eradication of Triple-Negative Breast Cancer Cells by Targeting Glycosylated PD-L1.Cancer cell · 2018Article
- Identification of a novel substance P (SP)-neurokinin-1 receptor (NK-1R) microRNA-221-5p inflammatory network in human colonic epithelial cells.Cellular and molecular gastroenterology and hepatology · 2015Article
- Functional Divergence in the Role of N-Linked Glycosylation in Smoothened Signaling.PLoS genetics · 2015Article
- Targeting NK-1 Receptors to Prevent and Treat Pancreatic Cancer: a New Therapeutic Approach.Cancers · 2015Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18. We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites. Using a lentiviral transfection system, the mutants were stably transfected into NCM 460 cells, a nontransformed human colonic epithelial cell line. We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation. All mutant receptors were able to bind to substance P and neurokinin A ligand with similar affinities; however, the double mutant, nonglycosylated NK1R showed only half the B(max) of the wild-type NK1R. In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion. All mutants were able to internalize, but the kinetics of internalization of the double mutant receptor was more rapid, when compared with wild-type NK1R. Therefore, glycosylation of NK1R may stabilize the receptor in the plasma membrane. These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
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