ArticleMolecular and cellular biology2007
N-cadherin is an in vivo substrate for protein tyrosine phosphatase sigma (PTPsigma) and participates in PTPsigma-mediated inhibition of axon growth.
Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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
32 citing papers in PubMed, 55 citations in OpenAlex.
- Article
- Type IIa RPTPs and Glycans: Roles in Axon Regeneration and Synaptogenesis.International journal of molecular sciences · 2021Review
- LAR Receptor Tyrosine Phosphatase Family in Healthy and Diseased Brain.Frontiers in cell and developmental biology · 2021Review
- Regulation of autophagy by inhibitory CSPG interactions with receptor PTPσ and its impact on plasticity and regeneration after spinal cord injury.Experimental neurology · 2020Review
- Article
- Advances in the Signaling Pathways Downstream of Glial-Scar Axon Growth Inhibitors.Frontiers in cellular neuroscience · 2020Review
- Mechanisms of PTPσ-Mediated Presynaptic Differentiation.Frontiers in synaptic neuroscience · 2019Article
- Two receptor tyrosine phosphatases dictate the depth of axonal stabilizing layer in the visual system.eLife · 2017Article
- Regulation of Drosophila Brain Wiring by Neuropil Interactions via a Slit-Robo-RPTP Signaling Complex.Developmental cell · 2016Article
- Targeting phosphatase-dependent proteoglycan switch for rheumatoid arthritis therapy.Science translational medicine · 2015Article
- Angiomotin is a novel component of cadherin-11/β-catenin/p120 complex and is critical for cadherin-11-mediated cell migration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- Extracellular regulation of type IIa receptor protein tyrosine phosphatases: mechanistic insights from structural analyses.Seminars in cell & developmental biology · 2015Review
- Integrating virtual and biochemical screening for protein tyrosine phosphatase inhibitor discovery.Methods (San Diego, Calif.) · 2014Article
- Protein tyrosine phosphatase σ targets apical junction complex proteins in the intestine and regulates epithelial permeability.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Influence of the extracellular matrix on endogenous and transplanted stem cells after brain damage.Frontiers in cellular neuroscience · 2014Review
- Protein tyrosine phosphatases PTPδ, PTPσ, and LAR: presynaptic hubs for synapse organization.Trends in neurosciences · 2013Review
- Structure of the catalytic domain of protein tyrosine phosphatase sigma in the sulfenic acid form.Molecules and cells · 2013Article
- Protein tyrosine phosphatase receptor type O inhibits trigeminal axon growth and branching by repressing TrkB and Ret signaling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Protein tyrosine phosphatase σ in proteoglycan-mediated neural regeneration regulation.Molecular neurobiology · 2013Review
- Identification of small molecule inhibitors of PTPσ through an integrative virtual and biochemical approach.PloS one · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein tyrosine phosphatase sigma (PTPsigma) belongs to the LAR family of receptor tyrosine phosphatases and was previously shown to negatively regulate axon growth. The substrate for PTPsigma and the effector(s) mediating this inhibitory effect were unknown. Here we report the identification of N-cadherin as an in vivo substrate for PTPsigma. Using brain lysates from PTPsigma knockout mice, in combination with substrate trapping, we identified a hyper-tyrosine-phosphorylated protein of approximately 120 kDa in the knockout animals (relative to sibling controls), which was identified by mass spectrometry and immunoblotting as N-cadherin. beta-Catenin also precipitated in the complex and was also a substrate for PTPsigma. Dorsal root ganglion (DRG) neurons, which highly express endogenous N-cadherin and PTPsigma, exhibited a faster growth rate in the knockout mice than in the sibling controls when grown on laminin or N-cadherin substrata. However, when N-cadherin function was disrupted by an inhibitory peptide or lowering calcium concentrations, the differential growth rate between the knockout and sibling control mice was greatly diminished. These results suggest that the elevated tyrosine phosphorylation of N-cadherin in the PTPsigma(-/-) mice likely disrupted N-cadherin function, resulting in accelerated DRG nerve growth. We conclude that N-cadherin is a physiological substrate for PTPsigma and that N-cadherin (and likely beta-catenin) participates in PTPsigma-mediated inhibition of axon growth.
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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.