ArticlePloS one2009
HD-PTP is a catalytically inactive tyrosine phosphatase due to a conserved divergence in its phosphatase domain.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 54 citations in OpenAlex.
- Bridging Manual and Computational Approaches: The Pseudophosphatase Scanner for Genome-Wide Fungal Pseudophosphatome Analysis.ACS omega · 2026Article
- PTPN23-dependent activation of PI3KC2α is a therapeutic vulnerability of BRAF-mutant cancers.The Journal of experimental medicine · 2025Article
- Loss of HD-PTP function results in lipodystrophy, defective cellular signaling and altered lipid homeostasis.Journal of cell science · 2024Article
- Ptpn23 Controls Cardiac T-Tubule Patterning by Promoting the Assembly of Dystrophin-Glycoprotein Complex.Circulation · 2024Article
- Genetic Variants in Protein Tyrosine Phosphatase Non-Receptor Type 23 Are Responsible for Mesiodens Formation.Biology · 2023Article
- Endofin is required for HD-PTP and ESCRT-0 interdependent endosomal sorting of ubiquitinated transmembrane cargoes.iScience · 2021Article
- His domain protein tyrosine phosphatase and Rabaptin-5 couple endo-lysosomal sorting of EGFR with endosomal maturation.Journal of cell science · 2021Article
- The Roles of Pseudophosphatases in Disease.International journal of molecular sciences · 2021Review
- Final Exon Frameshift BiallelicBrain sciences · 2021Article
- Protein Tyrosine Phosphatases: A new paradigm in an old signaling system?Advances in cancer research · 2021Review
- The receptor PTPRU is a redox sensitive pseudophosphatase.Nature communications · 2020Article
- Developmental epileptic encephalopathy with hypomyelination and brain atrophy associated with PTPN23 variants affecting the assembly of UsnRNPs.European journal of human genetics : EJHG · 2018Article
- Myopic (HD-PTP, PTPN23) selectively regulates synaptic neuropeptide release.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Mutations of PTPN23 in developmental and epileptic encephalopathy.Human genetics · 2017Article
- Suppression of protein tyrosine phosphatase N23 predisposes to breast tumorigenesis via activation of FYN kinase.Genes & development · 2017Article
- UsnRNP biogenesis: mechanisms and regulation.Chromosoma · 2017Review
- Multifaceted Roles of ALG-2 in Ca(2+)-Regulated Membrane Trafficking.International journal of molecular sciences · 2016Review
- The catalytically inactive tyrosine phosphatase HD-PTP/PTPN23 is a novel regulator of SMN complex localization.Molecular biology of the cell · 2015Article
- Tumor-suppressive function of protein-tyrosine phosphatase non-receptor type 23 in testicular germ cell tumors is lost upon overexpression of miR142-3p microRNA.The Journal of biological chemistry · 2013Article
- Protein tyrosine phosphatases: structure, function, and implication in human disease.Methods in molecular biology (Clifton, N.J.) · 2013Review
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundThe HD-PTP protein has been described as a tumor suppressor candidate and based on its amino acid sequence, categorized as a classical non-transmembrane protein tyrosine phosphatase (PTP). To date, no HD-PTP phosphorylated substrate has been identified and controversial results concerning its catalytic activity have been recently reported. METHODOLOGY AND
resultsHere we report a rigorous enzymatic analysis demonstrating that the HD-PTP protein does not harbor tyrosine phosphatase or lipid phosphatase activity using the highly sensitive DiFMUP substrate and a panel of different phosphatidylinositol phosphates. We found that HD-PTP tyrosine phosphatase inactivity is caused by an evolutionary conserved amino acid divergence of a key residue located in the HD-PTP phosphatase domain since its back mutation is sufficient to restore the HD-PTP tyrosine phosphatase activity. Moreover, in agreement with a tumor suppressor activity, HD-PTP expression leads to colony growth reduction in human cancer cell lines, independently of its catalytic PTP activity status.
conclusionIn summary, we demonstrate that HD-PTP is a catalytically inactive protein tyrosine phosphatase. As such, we identify one residue involved in its inactivation and show that its colony growth reduction activity is independent of its PTP activity status in human cancer cell lines.
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