ArticleMolecular and cellular biology2007
Dimerization of protein tyrosine phosphatase sigma governs both ligand binding and isoform specificity.
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 21 papers.
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Who cites it
21 citing papers in PubMed.
- Structure-Based Engineering for PTPσ-Targeted Therapeutic Development.International journal of molecular sciences · 2026Review
- Structure-Based Engineering of a PTPsigma Ectodomain for Enhanced Solubility and Productivity.International journal of molecular sciences · 2025Article
- Detailed analyses of the crucial functions of Zn transporter proteins in alkaline phosphatase activation.The Journal of biological chemistry · 2020Article
- Regulatory Mechanisms and Novel Therapeutic Targeting Strategies for Protein Tyrosine Phosphatases.Chemical reviews · 2018Review
- Proteinaceous Regulators and Inhibitors of Protein Tyrosine Phosphatases.Molecules (Basel, Switzerland) · 2018Review
- Structural basis of SALM5-induced PTPδ dimerization for synaptic differentiation.Nature communications · 2018Article
- Identification of function-regulating antibodies targeting the receptor protein tyrosine phosphatase sigma ectodomain.PloS one · 2017Article
- Aging is associated with dimerization and inactivation of the brain-enriched tyrosine phosphatase STEP.Neurobiology of aging · 2016Article
- A Synthetic Lethal Screen Identifies a Role for Lin-44/Wnt in C. elegans Embryogenesis.PloS one · 2015Article
- Receptor protein tyrosine phosphatase σ binds to neurons in the adult mouse brain.Experimental neurology · 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
- Article
- Protein tyrosine phosphatase σ in proteoglycan-mediated neural regeneration regulation.Molecular neurobiology · 2013Review
- Receptor-type tyrosine phosphatase ligands: looking for the needle in the haystack.The FEBS journal · 2013Review
- Oxidative stress-induced oligomerization inhibits the activity of the non-receptor tyrosine phosphatase STEP61.Journal of neurochemistry · 2011Article
- Laforin, a dual specificity phosphatase involved in Lafora disease, is present mainly as monomeric form with full phosphatase activity.PloS one · 2011Article
- PTPBR7 binding proteins in myelinating neurons of the mouse brain.International journal of biological sciences · 2011Article
- The receptor protein tyrosine phosphatase LAR promotes R7 photoreceptor axon targeting by a phosphatase-independent signaling mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Dimerization of tyrosine phosphatase PTPRO decreases its activity and ability to inactivate TrkC.Journal of neurochemistry · 2009Article
- Article
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Authors and funding
7 authors.
Funding
Abstract
Signaling through receptor protein tyrosine phosphatases (RPTPs) can influence diverse processes, including axon development, lymphocyte activation, and cell motility. The molecular regulation of these enzymes, however, is still poorly understood. In particular, it is not known if, or how, the dimerization state of RPTPs is related to the binding of extracellular ligands. Protein tyrosine phosphatase sigma (PTPsigma) is an RPTP with major isoforms that differ in their complements of fibronectin type III domains and in their ligand-binding specificities. In this study, we show that PTPsigma forms homodimers in the cell, interacting at least in part through the transmembrane region. Using this knowledge, we provide the first evidence that PTPsigma ectodomains must be presented as dimers in order to bind heterophilic ligands. We also provide evidence of how alternative use of fibronectin type III domain complements in two major isoforms of PTPsigma can alter the ligand binding specificities of PTPsigma ectodomains. The data suggest that the alternative domains function largely to change the rotational conformations of the amino-terminal ligand binding sites of the ectodomain dimers, thus imparting novel ligand binding properties. These findings have important implications for our understanding of how heterophilic ligands interact with, and potentially regulate, RPTPs.
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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.