ArticleJournal of cell science2013
Multi-functional norrin is a ligand for the LGR4 receptor.
Article in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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.
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Who cites it
50 citing papers in PubMed, 83 citations in OpenAlex.
- Regulatory mechanisms of LGR4 on cancer and cancer stem cell properties.Discover oncology · 2026Review
- Enhancement of a nuclear factor of activated T cells (NFAT) reporter for the study of G protein-coupled receptors.Communications biology · 2026Article
- Cryo-EM structure of the full-length LGR4-RSPOs complex and a targeting nanobody for anti-obesity therapy.Nature communications · 2025Article
- Distinct structural mechanisms of LGR4 modulation by Norrin and RSPOs in Wnt/β-catenin signaling.Nature communications · 2025Article
- Importin-alpha transports Norrin to the nucleus to promote proliferation and Notch signaling in glioblastoma stem cells.Oncogene · 2025Article
- Rescue of cochlear vascular pathology prevents sensory hair cell loss in Norrie disease.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- LGR signaling mediates muscle-adipose tissue crosstalk and protects against diet-induced insulin resistance.Nature communications · 2024Article
- Reduction of specific enterocytes from loss of intestinal LGR4 improves lipid metabolism in mice.Nature communications · 2024Article
- LGR4: A New Receptor Member in Endocrine and Metabolic Diseases.Endocrine reviews · 2023Review
- LGR4 and LGR5 form distinct homodimers that only LGR4 complexes with RNF43/ZNRF3 to provide high affinity binding of R-spondin ligands.Scientific reports · 2023Article
- Crystal structure of LGR ligand α2/β5 fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- LGR4, a G Protein-Coupled Receptor With a Systemic Role: From Development to Metabolic Regulation.Frontiers in endocrinology · 2022Review
- Retinoschisis and Norrie disease: a missing link.BMC research notes · 2021Article
- The Role of LGR4 (GPR48) in Normal and Cancer Processes.International journal of molecular sciences · 2021Review
- Notch signaling is a critical initiator of roof plate formation as revealed by the use of RNA profiling of the dorsal neural tube.BMC biology · 2021Article
- Emerging Roles for LGR4 in Organ Development, Energy Metabolism and Carcinogenesis.Frontiers in genetics · 2021Review
- Function and therapeutic potential of G protein-coupled receptors in epididymis.British journal of pharmacology · 2020Review
- Norrin mediates opposing effects on tumor progression of glioblastoma stem cells.The Journal of clinical investigation · 2020Article
- Norrin mediates tumor-promoting and -suppressive effects in glioblastoma via Notch and Wnt.The Journal of clinical investigation · 2020Article
- Endogenous Wnt/β-catenin signaling in Müller cells protects retinal ganglion cells from excitotoxic damage.Molecular vision · 2020Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Mammalian LGR4, 5 and 6 are seven-transmembrane receptors that are important for diverse physiological processes. These receptors are orthologous to DLGR2, a Drosophila receptor activated by the burs/pburs heterodimer important for morphogenesis. Although recent studies indicated that four R-spondin proteins are cognate ligands for LGR4, 5 and 6 receptors, several BMP antagonists in vertebrates have been postulated to be orthologous to burs and pburs. Using newly available genome sequences, we showed that norrin is a vertebrate ortholog for insect burs and pburs and stimulates Wnt signaling mediated by LGR4, but not by LGR5 and 6, in mammalian cells. Although norrin could only activate LGR4, binding studies suggested interactions between norrin and LGR4, 5 and 6. Norrin, the Norrie disease gene product, is also capable of activating Wnt signaling mediated by the Frizzled4 receptor and serves as a BMP antagonist. Mutagenesis studies indicated that different norrin mutations found in patients with Norrie disease can be categorized into subgroups according to defects for signaling through the three distinct binding proteins. Thus, norrin is a rare ligand capable of binding three receptors/binding proteins that are important for BMP and Wnt signaling pathways.
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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.