ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2005
A novel substrate of receptor tyrosine phosphatase PTPRO is required for nerve growth factor-induced process outgrowth.
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 16 papers.
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Who cites it
16 citing papers in PubMed, 24 citations in OpenAlex.
- PTPRO Governs Synaptic Density, Long-Term Potentiation and Cognitive Function In Vivo.Neuroscience bulletin · 2026Article
- Protein tyrosine phosphatase PTPRO represses lung adenocarcinoma progression by inducing mitochondria-dependent apoptosis and restraining tumor metastasis.Cell death & disease · 2024Article
- Age-related decline in hippocampal tyrosine phosphatase PTPRO is a mechanistic factor in chemotherapy-related cognitive impairment.JCI insight · 2023Article
- Identification of Protein Tyrosine Phosphatase Receptor Type O (PTPRO) as a Synaptic Adhesion Molecule that Promotes Synapse Formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- PTPRO represses ERBB2-driven breast oncogenesis by dephosphorylation and endosomal internalization of ERBB2.Oncogene · 2017Article
- Neuronal pentraxin 1 negatively regulates excitatory synapse density and synaptic plasticity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- Protein tyrosine phosphatase receptor type O (Ptpro) regulates cerebellar formation during zebrafish development through modulating Fgf signaling.Cellular and molecular life sciences : CMLS · 2013Article
- Expression profiling during mammary epithelial cell three-dimensional morphogenesis identifies PTPRO as a novel regulator of morphogenesis and ErbB2-mediated transformation.Molecular and cellular biology · 2012Article
- Interaction of an intracellular pentraxin with a BTB-Kelch protein is associated with ubiquitylation, aggregation and neuronal apoptosis.Molecular and cellular neurosciences · 2011Article
- Gene expression profiles of HIV-1-infected glia and brain: toward better understanding of the role of astrocytes in HIV-1-associated neurocognitive disorders.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2010Review
- Dimerization of tyrosine phosphatase PTPRO decreases its activity and ability to inactivate TrkC.Journal of neurochemistry · 2009Article
- Antibodies to protein tyrosine phosphatase receptor type O (PTPro) increase glomerular albumin permeability (P(alb)).American journal of physiology. Renal physiology · 2009Article
- PPTX, a pentraxin domain-containing protein, interacts with the T1 domain of K v 4.Journal of neuroscience research · 2009Article
- Identification and correction of abnormal, incomplete and mispredicted proteins in public databases.BMC bioinformatics · 2008Article
- Neuronal pentraxin 1 contributes to the neuronal damage evoked by amyloid-beta and is overexpressed in dystrophic neurites in Alzheimer's brain.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- Receptor tyrosine phosphatases guide vertebrate motor axons during development.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2005Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The receptor protein tyrosine phosphatase PTPRO may be involved in axon guidance both as a ligand and as a neuronal receptor. We have begun to characterize signaling by PTPRO as a receptor by screening for proteins interacting with the intracellular domain of PTPRO. In a yeast-two hybrid screen, we identified a novel class of protein, which we named neuronal pentraxin with chromo domain (NPCD), as a PTPRO-interacting protein. We have shown recently that NPCD has multiple cytoplasmic isoforms as a result of alternative splicing and that these proteins are present in many neurons, mainly associated with the inner side of the plasma membrane. Through additional two-hybrid experiments, cotransfection and reciprocal coprecipitation, glutathione S-transferase pulldown, and immunoprecipitation in vivo, we confirm that NPCD isoforms interact with the catalytic phosphatase domain of PTPRO. We also find that at least one NPCD isoform is tyrosine phosphorylated in vivo and can serve as a substrate for PTPRO in vitro. Analysis of PTPRO knock-out mice demonstrates that normal localization of NPCD at the plasma membrane requires PTPRO expression, suggesting a physiological role for the NPCD/PTPRO interaction. NPCD is likely to be relevant to axon growth and/or guidance, because RNA interference mediated knock-down of NPCD expression in pheochromocytoma cells inhibits NGF-induced neuronal process outgrowth without affecting NGF-dependent survival or initial NGF signaling.
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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.