ArticleThe Journal of biological chemistry2015
LINGO-1 protein interacts with the p75 neurotrophin receptor in intracellular membrane compartments.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Epitranscriptomic imprints on glial cell polarization: METTL3/IGF2BP2 axis as a driver of neurodegeneration in Alzheimer's disease.Psychopharmacology · 2026Review
- B-cells expressing NgR1 and NgR3 are localized to EAE-induced inflammatory infiltrates and are stimulated by BAFF.Scientific reports · 2021Article
- Revising the mechanism of p75NTR activation: intrinsically monomeric state of death domains invokes the "helper" hypothesis.Scientific reports · 2020Article
- Opicinumab: is it a potential treatment for multiple sclerosis?Annals of translational medicine · 2020Article
- Electroacupuncture Promoting Axonal Regeneration in Spinal Cord Injury Rats via Suppression of Nogo/NgR and Rho/ROCK Signaling Pathway.Neuropsychiatric disease and treatment · 2019Article
- Defining the transcriptomic landscape of the developing enteric nervous system and its cellular environment.BMC genomics · 2017Article
- Spatiotemporal and Long Lasting Modulation of 11 Key Nogo Signaling Genes in Response to Strong Neuroexcitation.Frontiers in molecular neuroscience · 2017Article
- APP Receptor? To Be or Not To Be.Trends in pharmacological sciences · 2016Review
- Intracellular LINGO-1 negatively regulates Trk neurotrophin receptor signaling.Molecular and cellular neurosciences · 2016Article
- Assembly of Neuronal Connectivity by Neurotrophic Factors and Leucine-Rich Repeat Proteins.Frontiers in cellular neuroscience · 2016Review
- Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Axon outgrowth inhibition in response to trauma is thought to be mediated via the binding of myelin-associated inhibitory factors (e.g. Nogo-66, myelin-associated glycoprotein, oligodendrocyte myelin glycoprotein, and myelin basic protein) to a putative tripartite LINGO-1·p75(NTR)·Nogo-66 receptor (NgR) complex at the cell surface. We found that endogenous LINGO-1 expression in neurons in the cortex and cerebellum is intracellular. Mutation or truncation of the highly conserved LINGO-1 C terminus altered this intracellular localization, causing poor intracellular retention and increased plasma membrane expression. p75(NTR) associated predominantly with natively expressed LINGO-1 containing immature N-glycans, characteristic of protein that has not completed trans-Golgi-mediated processing, whereas mutant forms of LINGO-1 with enhanced plasma membrane expression did not associate with p75(NTR). Co-immunoprecipitation experiments demonstrated that LINGO-1 and NgR competed for binding to p75(NTR) in a manner that is difficult to reconcile with the existence of a LINGO-1·p75(NTR)·NgR ternary complex. These findings contradict models postulating functional LINGO-1·p75(NTR)·NgR complexes in the plasma membrane.
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