ArticlePloS one2012
Regulation of GIP and GLP1 receptor cell surface expression by N-glycosylation and receptor heteromerization.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
34 citing papers in PubMed, 1 synthesis or guideline pooled it, 60 citations in OpenAlex.
- GIP as a Potential Therapeutic Target for Atherosclerotic Cardiovascular Disease-A Systematic Review.International journal of molecular sciences · 2020Pooled it
- The Role and Mechanism of Incretins in Gynaecologic Diseases.Endocrinology, diabetes & metabolism · 2026Review
- Transmembrane E3 ligase RNF128 regulates N-glycosylation by promoting ribophorin I ubiquitination and degradation.BMB reports · 2024Article
- Does glucose-dependent insulinotropic polypeptide receptor blockade as well as agonism have a role to play in management of obesity and diabetes?The Journal of endocrinology · 2024Review
- Blood pH Analysis in Combination with Molecular Medical Tools in Relation to COVID-19 Symptoms.Biomedicines · 2023Article
- New Insights into the Structure and Function of Class B1 GPCRs.Endocrine reviews · 2023Article
- Rapid One-Step Capturing of Native, Cell-Free Synthesized and Membrane-Embedded GLP-1R.International journal of molecular sciences · 2023Article
- Variation in responses to incretin therapy: Modifiable and non-modifiable factors.Frontiers in molecular biosciences · 2023Review
- Differential effects of glucose-dependent insulinotropic polypeptide receptor/glucagon-like peptide-1 receptor heteromerization on cell signaling when expressed in HEK-293 cells.Pharmacology research & perspectives · 2022Article
- Post-Translational Modifications of G Protein-Coupled Receptors Revealed by Proteomics and Structural Biology.Frontiers in chemistry · 2022Review
- Role of a Dual Glucose-Dependent Insulinotropic Peptide (GIP)/Glucagon-like Peptide-1 Receptor Agonist (Twincretin) in Glycemic Control: From Pathophysiology to Treatment.Life (Basel, Switzerland) · 2021Review
- GIPR antagonist antibodies conjugated to GLP-1 peptide are bispecific molecules that decrease weight in obese mice and monkeys.Cell reports. Medicine · 2021Article
- Protein Glycosylation in Diabetes.Advances in experimental medicine and biology · 2021Article
- G Protein-Coupled Receptors in the Sweet Spot: Glycosylation and other Post-translational Modifications.ACS pharmacology & translational science · 2020Review
- Calcitonin Receptor N-Glycosylation Enhances Peptide Hormone Affinity by Controlling Receptor Dynamics.Journal of molecular biology · 2020Article
- The Effect of Cell Surface Expression and Linker Sequence on the Recruitment of Arrestin to the GIP Receptor.Frontiers in pharmacology · 2020Article
- Agonist-induced membrane nanodomain clustering drives GLP-1 receptor responses in pancreatic beta cells.PLoS biology · 2019Article
- Simultaneous analyses of carbohydrate-mediated serum GLP-1 and GLP-2 and duodenal receptor expression in children with and without celiac disease.Therapeutic advances in gastroenterology · 2019Article
- Article
- Pleiotropic Effects of GLP-1 and Analogs on Cell Signaling, Metabolism, and Function.Frontiers in endocrinology · 2018Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In response to a meal, Glucose-dependent Insulinotropic Polypeptide (GIP) and Glucagon-like Peptide-1 (GLP-1) are released from gut endocrine cells into the circulation and interact with their cognate G-protein coupled receptors (GPCRs). Receptor activation results in tissue-selective pleiotropic responses that include augmentation of glucose-induced insulin secretion from pancreatic beta cells. N-glycosylation and receptor oligomerization are co-translational processes that are thought to regulate the exit of functional GPCRs from the ER and their maintenance at the plasma membrane. Despite the importance of these regulatory processes, their impact on functional expression of GIP and GLP-1 receptors has not been well studied. Like many family B GPCRs, both the GIP and GLP-1 receptors possess a large extracellular N-terminus with multiple consensus sites for Asn-linked (N)-glycosylation. Here, we show that each of these Asn residues is glycosylated when either human receptor is expressed in Chinese hamster ovary cells. N-glycosylation enhances cell surface expression and function in parallel but exerts stronger control over the GIP receptor than the GLP-1 receptor. N-glycosylation mainly lengthens receptor half-life by reducing degradation in the endoplasmic reticulum. N-glycosylation is also required for expression of the GIP receptor at the plasma membrane and efficient GIP potentiation of glucose-induced insulin secretion from the INS-1 pancreatic beta cell line. Functional expression of a GIP receptor mutant lacking N-glycosylation is rescued by co-expressed wild type GLP1 receptor, which, together with data obtained using Bioluminescence Resonance Energy Transfer, suggests formation of a GIP-GLP1 receptor heteromer.
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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.