ArticleMolecular oncology2016
Unbiased identification of substrates of protein tyrosine phosphatase ptp-3 in C. elegans.
Article in Molecular oncology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 20 citations in OpenAlex.
- Machine learning-driven prediction of substrates for enzymes introducing or removing protein post-translational modifications.Communications chemistry · 2025Article
- Ptprd deficiency promotes tau hyperphosphorylation and impairs cognitive function in aged mice.Biological research · 2025Article
- Kinome-wide RNAi screening inJournal of biosciences · 2025Article
- Catalytic activities of wild-type C. elegans DAF-2 kinase and dauer-associated mutants.The FEBS journal · 2024Article
- Cell Cycle-Specific Protein Phosphatase 1 (PP1) Substrates Identification Using Genetically Modified Cell Lines.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Substrate-selective positive allosteric modulation of PTPRD's phosphatase by flavonols.Biochemical pharmacology · 2022Article
- l-Lactate Dehydrogenase Identified as a Protein Tyrosine Phosphatase 1B Substrate by Using K-BIPS.Chembiochem : a European journal of chemical biology · 2021Article
- LAR Receptor Tyrosine Phosphatase Family in Healthy and Diseased Brain.Frontiers in cell and developmental biology · 2021Review
- PTP-3 phosphatase promotes intramolecular folding of SYD-2 to inactivate kinesin-3 UNC-104 in neurons.Molecular biology of the cell · 2020Article
- Spatial confinement of receptor activity by tyrosine phosphatase during directional cell migration.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- MET targeting: time for a rematch.Oncogene · 2020Review
- PTPRD: neurobiology, genetics, and initial pharmacology of a pleiotropic contributor to brain phenotypes.Annals of the New York Academy of Sciences · 2019Review
- Cocaine reward is reduced by decreased expression of receptor-type protein tyrosine phosphatase D (PTPRD) and by a novel PTPRD antagonist.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Protein Tyrosine Phosphatase δ Mediates the Sema3A-Induced Cortical Basal Dendritic Arborization through the Activation of Fyn Tyrosine Kinase.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- Unbiased identification of substrates of protein tyrosine phosphatase ptp-3 in C. elegans.Molecular oncology · 2016Article
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Authors and funding
6 authors at 1 institution in 2 countries.
Funding
Abstract
The leukocyte antigen related (LAR) family of receptor-like protein tyrosine phosphatases has three members in humans - PTPRF, PTPRD and PTPRS - that have been implicated in diverse processes including embryonic development, inhibition of cell growth and axonal guidance. Mutations in the LAR family are associated with developmental defects such as cleft palate as well as various cancers including breast, neck, lung, colon and brain. Although this family of tyrosine phosphatases is important for many developmental processes, little is known of their substrates. This is partially due to functional redundancy within the LAR family, as deletion of a single gene in the LAR family does not have an appreciable phenotype, but a dual knockout is embryonically lethal in mouse models. To circumvent the inability to knockout multiple members of the LAR family in mouse models, we used a knockout of ptp-3, which is the only known ortholog of the LAR family in Caenorhabditis elegans and allows for the study of the LAR family at the organismal level. Using SILAC-based quantitative phosphoproteomics, we identified 255 putative substrates of ptp-3, which included four of the nine known annotated substrates of the LAR family. A motif analysis of the identified phosphopeptides allowed for the determination of sequences that appear to be preferentially dephosphorylated. Finally, we discovered that kinases were overrepresented in the list of identified putative substrates and tyrosine residues whose phosphorylation is known to increase kinase activity were dephosphorylated by ptp-3. These data are suggestive of ptp-3 as a potential negative regulator of several kinase families, such as the mitogen activated kinases (MAPKs), and multiple tyrosine kinases including FER, MET, and NTRK2.
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