ArticleThe Journal of biological chemistry2011
Receptor-like protein-tyrosine phosphatase α enhances cell surface expression of neural adhesion molecule NB-3.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- CNTN6 Modulates Slit-Robo Signaling in Cortical GABAergic Interneuron Migration.Neuroscience bulletin · 2026Article
- Cell Adhesion Molecules Involved in Neurodevelopmental Pathways Implicated in 3p-Deletion Syndrome and Autism Spectrum Disorder.Frontiers in cellular neuroscience · 2020Review
- Latrophilin's Social Protein Network.Frontiers in neuroscience · 2019Review
- Glial and Neuronal Protein Tyrosine Phosphatase Alpha (PTPα) Regulate Oligodendrocyte Differentiation and Myelination.Journal of molecular neuroscience : MN · 2017Article
- Developmental role of the cell adhesion molecule Contactin-6 in the cerebral cortex and hippocampus.Cell adhesion & migration · 2016Article
- Association of Cell Adhesion Molecules Contactin-6 and Latrophilin-1 Regulates Neuronal Apoptosis.Frontiers in molecular neuroscience · 2016Article
- Neuronal migration and its disorders affecting the CA3 region.Frontiers in cellular neuroscience · 2014Review
- Protein tyrosine phosphatase α in the dorsomedial striatum promotes excessive ethanol-drinking behaviors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Contactin 4, -5 and -6 differentially regulate neuritogenesis while they display identical PTPRG binding sites.Biology open · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 5 institutions in 4 countries.
Funding
Abstract
Neural adhesion molecule NB-3 plays an important role in the apical dendrite development of layer V pyramidal neurons in the visual cortex, and receptor-like protein-tyrosine phosphatase α (PTPα) mediates NB-3 signaling in this process. Here we investigated the role of PTPα in regulating cell surface expression of NB-3. We found that cortical neurons from PTPα knock-out mice exhibited a lower level of NB-3 at the cell surface. When expressed in COS1 cells, NB-3 was enriched in the Golgi apparatus with a low level of cell surface expression. However, co-expression of PTPα increased the cell surface distribution of NB-3. Further analysis showed that PTPα facilitated Golgi exit of NB-3 and stabilized NB-3 protein at the cell surface by preventing its release from the plasma membrane. The extracellular region of PTPα but not its catalytic activity is necessary for its effect on NB-3 expression. Thus, the PTPα-mediated increase of NB-3 level at the cell surface represents a novel function of PTPα in NB-3 signaling in neural development.
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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.