ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2005
The Nogo-66 receptor homolog NgR2 is a sialic acid-dependent receptor selective for myelin-associated glycoprotein.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.
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Who cites it
114 citing papers in PubMed, 228 citations in OpenAlex.
- Myelin dysfunction in autism spectrum disorder: insights into core symptoms and mechanisms of brain development.Molecular psychiatry · 2026Review
- Probing the role of synaptic adhesion molecule RTN4RL2 in setting up cochlear connectivity.eLife · 2025Article
- A novel sialylation pathway mediated by extracellular vesicles in aggressive prostate cancer.PloS one · 2025Article
- Expression of the αVβ3 integrin affects prostate cancer sEV cargo and density and promotes sEV pro-tumorigenic activity in vivo through a GPI-anchored receptor, NgR2.Journal of extracellular vesicles · 2024Article
- Differential expression of genes in the RhoA/ROCK pathway in the hippocampus and cortex following intermittent hypoxia and high-intensity interval training.Journal of neurophysiology · 2024Article
- Axonal growth inhibitors and their receptors in spinal cord injury: from biology to clinical translation.Neural regeneration research · 2023Review
- Targeting the αVβ3/NgR2 pathway in neuroendocrine prostate cancer.Matrix biology : journal of the International Society for Matrix Biology · 2023Article
- NgR1 binding to reovirus reveals an unusual bivalent interaction and a new viral attachment protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The NOGO receptor NgR2, a novel αVβ3 integrin effector, induces neuroendocrine differentiation in prostate cancer.Scientific reports · 2022Article
- Synaptic or Non-synaptic? Different Intercellular Interactions with Retinal Ganglion Cells in Optic Nerve Regeneration.Molecular neurobiology · 2022Review
- One Raft to Guide Them All, and in Axon Regeneration Inhibit Them.International journal of molecular sciences · 2021Review
- Transcriptome Profiling of Mouse Corpus Callosum After Cerebral Hypoperfusion.Frontiers in cell and developmental biology · 2021Article
- Advances in the Signaling Pathways Downstream of Glial-Scar Axon Growth Inhibitors.Frontiers in cellular neuroscience · 2020Review
- A Novel Siglec-4 Derived Spacer Improves the Functionality of CAR T Cells Against Membrane-Proximal Epitopes.Frontiers in immunology · 2020Article
- MAG induces apoptosis in cerebellar granule neurons through p75Cell death & disease · 2019Article
- Review
- Differences in neuroplasticity after spinal cord injury in varying animal models and humans.Neural regeneration research · 2019Review
- Integrins promote axonal regeneration after injury of the nervous system.Biological reviews of the Cambridge Philosophical Society · 2018Review
- An IFNγ/CXCL2 regulatory pathway determines lesion localization during EAE.Journal of neuroinflammation · 2018Article
- Nogo receptor expression in microglia/macrophages during experimental autoimmune encephalomyelitis progression.Neural regeneration research · 2018Article
54 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
The Nogo-66 receptor (NgR1) is a promiscuous receptor for the myelin inhibitory proteins Nogo/Nogo-66, myelin-associated glycoprotein (MAG), and oligodendrocyte myelin glycoprotein (OMgp). NgR1, an axonal glycoprotein, is the founding member of a protein family composed of the structurally related molecules NgR1, NgR2, and NgR3. Here we show that NgR2 is a novel receptor for MAG and acts selectively to mediate MAG inhibitory responses. MAG binds NgR2 directly and with greater affinity than NgR1. In neurons NgR1 and NgR2 support MAG binding in a sialic acid-dependent Vibrio cholerae neuraminidase-sensitive manner. Forced expression of NgR2 is sufficient to impart MAG inhibition to neonatal sensory neurons. Soluble NgR2 has MAG antagonistic capacity and promotes neuronal growth on MAG and CNS myelin substrate in vitro. Structural studies have revealed that the NgR2 leucine-rich repeat cluster and the NgR2 "unique" domain are necessary for high-affinity MAG binding. Consistent with its role as a neuronal MAG receptor, NgR2 is an axonassociated glycoprotein. In postnatal brain NgR1 and NgR2 are strongly enriched in Triton X-100-insoluble lipid rafts. Neural expression studies of NgR1 and NgR2 have revealed broad and overlapping, yet distinct, distribution in the mature CNS. Taken together, our studies identify NgRs as a family of receptors (or components of receptors) for myelin inhibitors and provide insights into how interactions between MAG and members of the Nogo receptor family function to coordinate myelin inhibitory responses.
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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.