ArticleThe Journal of cell biology1996
The neurotrophin receptor, gp75, forms a complex with the receptor tyrosine kinase TrkA.
Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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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
12 citing papers in PubMed, 67 citations in OpenAlex.
- Antibody and aptamer-based therapies for osteoarthritis: Application of antibodies and promise of aptamers.Molecular therapy. Nucleic acids · 2025Review
- High-affinity TrkA and p75 neurotrophin receptor complexes: A twisted affair.The Journal of biological chemistry · 2022Review
- Comparison of nerve growth factor receptor binding models using heterodimeric muteins.Journal of neuroscience research · 2012Article
- Proteolytic processing of the p75 neurotrophin receptor and two homologs generates C-terminal fragments with signaling capability.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003Article
- Molecular kinetics of nerve growth factor receptor trafficking and activation.The Journal of biological chemistry · 2002Article
- The extracellular domain of p75NTR is necessary to inhibit neurotrophin-3 signaling through TrkA.The Journal of biological chemistry · 2001Article
- An evolutionarily conserved transmembrane protein that is a novel downstream target of neurotrophin and ephrin receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001Article
- Signaling of neuronal cell death by the p75NTR neurotrophin receptor.Molecular neurobiology · 1999Review
- Biochemical and functional interactions between the neurotrophin receptors trk and p75NTR.The EMBO journal · 1999Article
- Absence of the p75 neurotrophin receptor alters the pattern of sympathosensory sprouting in the trigeminal ganglia of mice overexpressing nerve growth factor.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999Article
- The p75 neurotrophin receptor mediates neuronal apoptosis and is essential for naturally occurring sympathetic neuron death.The Journal of cell biology · 1998Article
- Optimal nerve growth factor trophic signals mediated by synergy of TrkA and p75 receptor-specific ligands.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1997Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The high-affinity NGF receptor is thought to be a complex of two receptors , gp75 and the tyrosine kinase TrkA, but direct biochemical evidence for such an association had been lacking. In this report, we demonstrate the existence of such a gp75-TrkA complex by a copatching technique. Gp75 on the surface of intact cells is patched with an anti-gp75 antibody and fluorescent secondary antibody, the cells are then fixed to prevent further antibody-induced redistributions, and the distribution of TrkA is probed with and anti-TrkA antibody and fluorescent secondary antibody. We utilize a baculovirus-insect cell expression of wild-type and mutated NGF receptors. TrkA and gp75 copatch in both the absence and presence of NGF. The association is specific, since gp75 does not copatch with other tyrosine kinase receptors, including TrkB, platelet-derived growth factor receptor-beta, and Torso (Tor). To determine which domains of TrkA are required for copatching, we used a series of TrkA-Tor chimeric receptors and show that the extracellular domain of TrkA is sufficient for copatching with gp75. A chimeric receptor with TrkA transmembrane and intracellular domains show partial copatching with gp75. Deletion of the intracellular domain of gp75 decreases but does not eliminate copatching. A point mutation which inactivates the TrkA kinase has no effect on copatching, indicating that this enzymatic activity is not required for association with gp75. Hence, although interactions between the gp75 and TrkA extracellular domains are sufficient for complex formation, interactions involving other receptor domains also play a role.
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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.