ArticleeLife2015
Structural basis of death domain signaling in the p75 neurotrophin receptor.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 96 citations in OpenAlex.
- p75 neurotrophin receptor signaling through the RhoA/ROCK pathway contributes to Tau-mediated neurodegeneration.Molecular psychiatry · 2026Article
- Molecular neurobiological insights on integrative role of Trk neurotrophic receptors and their small-molecule agonists in neurodegenerative conditions.Experimental brain research · 2026Review
- Structural and dynamic basis of NOD2 tandem CARD association and NOD1/2-RIP2 signaling complexes.PLoS computational biology · 2026Article
- Mammalian innate antiviral defenses: beyond interferon.Journal of virology · 2025Review
- Impaired migration and lung invasion of human melanoma by a novel small molecule targeting the transmembrane domain of death receptor p75EMBO molecular medicine · 2025Article
- Recent Advances in the Molecular Mechanisms of Ocular Dominance Plasticity in the Visual Cortex.Neuroscience bulletin · 2025Review
- Review
- ERCC1/NGFR affects prognosis in basal-like breast cancer.European journal of medical research · 2025Article
- A structural atlas of death domain fold proteins reveals their versatile roles in biology and function.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Current advances on RIPK2 and its inhibitors in pathological processes: a comprehensive review.Frontiers in molecular neuroscience · 2025Review
- What frog gill resorption brings: loss of function, cell death, and metabolic reorganization.Frontiers in zoology · 2024Article
- Article
- AraC interacts with p75Cell death & disease · 2023Article
- Recent advances in the development of RIPK2 modulators for the treatment of inflammatory diseases.Frontiers in pharmacology · 2023Review
- Differential contribution of TrkB and p75Frontiers in molecular neuroscience · 2023Article
- Immune activation of the p75 neurotrophin receptor: implications in neuroinflammation.Frontiers in molecular neuroscience · 2023Article
- Human immunomodulatory ligand B7-1 mediates synaptic remodeling via the p75 neurotrophin receptor.The Journal of clinical investigation · 2022Article
- High-affinity TrkA and p75 neurotrophin receptor complexes: A twisted affair.The Journal of biological chemistry · 2022Review
- A Structural and Functional Perspective of Death Receptor 6.Frontiers in pharmacology · 2022Review
- Electrostatic Forces Mediate the Specificity of RHO GTPase-GDI Interactions.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Death domains (DDs) mediate assembly of oligomeric complexes for activation of downstream signaling pathways through incompletely understood mechanisms. Here we report structures of complexes formed by the DD of p75 neurotrophin receptor (p75(NTR)) with RhoGDI, for activation of the RhoA pathway, with caspase recruitment domain (CARD) of RIP2 kinase, for activation of the NF-kB pathway, and with itself, revealing how DD dimerization controls access of intracellular effectors to the receptor. RIP2 CARD and RhoGDI bind to p75(NTR) DD at partially overlapping epitopes with over 100-fold difference in affinity, revealing the mechanism by which RIP2 recruitment displaces RhoGDI upon ligand binding. The p75(NTR) DD forms non-covalent, low-affinity symmetric dimers in solution. The dimer interface overlaps with RIP2 CARD but not RhoGDI binding sites, supporting a model of receptor activation triggered by separation of DDs. These structures reveal how competitive protein-protein interactions orchestrate the hierarchical activation of downstream pathways in non-catalytic receptors.
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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.