ArticleThe Journal of biological chemistry2011
Identification of new substrates of the protein-tyrosine phosphatase PTP1B by Bayesian integration of proteome evidence.
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 32 papers.
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Who cites it
32 citing papers in PubMed, 53 citations in OpenAlex.
- Distal Mutations Rewire Allosteric Networks to Control Substrate Specificity in PTP1B.Biochemistry · 2025Article
- Machine learning-driven prediction of substrates for enzymes introducing or removing protein post-translational modifications.Communications chemistry · 2025Article
- Uncovering Enzyme-Specific Post-Translational Modifications: An Overview of Current Methods.Proteomes · 2025Review
- PP2A-B56α is a key determinant of cardiac protein phosphorylation and functional responses to β-adrenergic signalling.Journal of molecular and cellular cardiology plus · 2025Article
- Allosteric regulation of the tyrosine phosphatase PTP1B by a protein-protein interaction.Protein science : a publication of the Protein Society · 2025Article
- A PTP1B-Cdk3 Signaling Axis Promotes Cell Cycle Progression of Human Glioblastoma Cells through an Rb-E2F Dependent Pathway.Molecular and cellular biology · 2023Article
- Tyrosine phosphatases regulate resistance to ALK inhibitors in ALK+ anaplastic large cell lymphoma.Blood · 2022Article
- Quantitative proteomics identifies PTP1B as modulator of B cell antigen receptor signaling.Life science alliance · 2021Article
- Targeting Degradation of EGFR through the Allosteric Site Leads to Cancer Cell Detachment-Promoted Death.Cancers · 2019Article
- The HSV-1 mechanisms of cell-to-cell spread and fusion are critically dependent on host PTP1B.PLoS pathogens · 2018Article
- Reactive Chemicals and Electrophilic Stress in Cancer: A Minireview.High-throughput · 2018Review
- Both Intrinsic Substrate Preference and Network Context Contribute to Substrate Selection of Classical Tyrosine Phosphatases.The Journal of biological chemistry · 2017Article
- Prediction and verification of novel peptide targets of protein tyrosine phosphatase 1B.Bioorganic & medicinal chemistry · 2016Article
- Increased PTP1B expression and phosphatase activity in colorectal cancer results in a more invasive phenotype and worse patient outcome.Oncotarget · 2016Article
- Activation of EGFR by small compounds through coupling the generation of hydrogen peroxide to stable dimerization of Cu/Zn SOD1.Scientific reports · 2016Article
- A tyrosine phosphatase SHP2 gain-of-function mutation enhances malignancy of breast carcinoma.Oncotarget · 2016Article
- Expression and clinical significance of tyrosine phosphatase SHP2 in thyroid carcinoma.Oncology letters · 2015Article
- 14-3-3-Pred: improved methods to predict 14-3-3-binding phosphopeptides.Bioinformatics (Oxford, England) · 2015Article
- UBC9-dependent association between calnexin and protein tyrosine phosphatase 1B (PTP1B) at the endoplasmic reticulum.The Journal of biological chemistry · 2015Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
There is growing evidence that tyrosine phosphatases display an intrinsic enzymatic preference for the sequence context flanking the target phosphotyrosines. On the other hand, substrate selection in vivo is decisively guided by the enzyme-substrate connectivity in the protein interaction network. We describe here a system wide strategy to infer physiological substrates of protein-tyrosine phosphatases. Here we integrate, by a Bayesian model, proteome wide evidence about in vitro substrate preference, as determined by a novel high-density peptide chip technology, and "closeness" in the protein interaction network. This allows to rank candidate substrates of the human PTP1B phosphatase. Ultimately a variety of in vitro and in vivo approaches were used to verify the prediction that the tyrosine phosphorylation levels of five high-ranking substrates, PLC-γ1, Gab1, SHP2, EGFR, and SHP1, are indeed specifically modulated by PTP1B. In addition, we demonstrate that the PTP1B-mediated dephosphorylation of Gab1 negatively affects its EGF-induced association with the phosphatase SHP2. The dissociation of this signaling complex is accompanied by a decrease of ERK MAP kinase phosphorylation and activation.
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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.