ArticleMolecular and cellular biology2009
New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival.
Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 80 citations in OpenAlex.
- The role of classical protein tyrosine phosphatases in diabetic kidney disease and therapeutic implications.Journal of biomedical science · 2026Review
- MiR-362-3p inhibits the proliferation, migration and EMT of gastric cancer cells by regulating the DEP-1/ERK signaling pathway.Scientific reports · 2026Article
- A mechanistic computational model of HGF-VEGF-mediated endothelial cell proliferation and vascular permeability.iScience · 2025Article
- Promoting vascular stability through Src inhibition and Tie2 activation: A model-based analysis.iScience · 2025Article
- CD148 agonistic antibody alleviates renal injury induced by chronic angiotensin II infusion in mice.BMC nephrology · 2025Article
- Meis1 Targets Protein Tyrosine Phosphatase Receptor J in Fibroblast to Retard Chronic Kidney Disease Progression.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Vascular endothelial cell morphology and alignment regulate VEGF-induced endothelial nitric oxide synthase activation.Cytoskeleton (Hoboken, N.J.) · 2024Article
- The receptor protein tyrosine phosphatase PTPRK promotes intestinal repair and catalysis-independent tumour suppression.Journal of cell science · 2024Article
- Pan-cancer Analysis Reveals SRC May Link Lipid Metabolism and Macrophages.Iranian journal of biotechnology · 2023Article
- The effects of CD148 Q276P/R326Q polymorphisms in A431D epidermoid cancer cell proliferation and epidermal growth factor receptor signaling.Cancer reports (Hoboken, N.J.) · 2022Article
- ERK and Akt exhibit distinct signaling responses following stimulation by pro-angiogenic factors.Cell communication and signaling : CCS · 2020Article
- Mathematical Model Predicts Effective Strategies to Inhibit VEGF-eNOS Signaling.Journal of clinical medicine · 2020Article
- Article
- Agonistic anti-CD148 monoclonal antibody attenuates diabetic nephropathy in mice.American journal of physiology. Renal physiology · 2020Article
- Growth Factor Deregulation and Emerging Role of Phosphatases in Diabetic Peripheral Artery Disease.Frontiers in cardiovascular medicine · 2020Review
- Disrupting the transmembrane domain-mediated oligomerization of protein tyrosine phosphatase receptor J inhibits EGFR-driven cancer cell phenotypes.The Journal of biological chemistry · 2019Article
- WMJ-S-001, a Novel Aliphatic Hydroxamate-Based Compound, Suppresses Lymphangiogenesis Through p38mapk-p53-survivin Signaling Cascade.Frontiers in oncology · 2019Article
- Mechanistic insight into activation of MAPK signaling by pro-angiogenic factors.BMC systems biology · 2018Article
- Somatic inactivating PTPRJ mutations and dysregulated pathways identified in canine malignant melanoma by integrated comparative genomic analysis.PLoS genetics · 2018Article
- Computer Simulation of TSP1 Inhibition of VEGF-Akt-eNOS: An Angiogenesis Triple Threat.Frontiers in physiology · 2018Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Functional inactivation of the protein tyrosine phosphatase DEP-1 leads to increased endothelial cell proliferation and failure of vessels to remodel and branch. DEP-1 has also been proposed to contribute to the contact inhibition of endothelial cell growth via dephosphorylation of vascular endothelial growth factor receptor 2 (VEGFR2), a mediator of vascular development. However, how DEP-1 regulates VEGF-dependent signaling and biological responses remains ill-defined. We show here that DEP-1 targets tyrosine residues in the VEGFR2 kinase activation loop. Consequently, depletion of DEP-1 results in the increased phosphorylation of all major VEGFR2 autophosphorylation sites, but surprisingly, not in the overall stimulation of VEGF-dependent signaling. The increased phosphorylation of Src on Y529 under these conditions results in impaired Src and Akt activation. This inhibition is similarly observed upon expression of catalytically inactive DEP-1, and coexpression of an active Src-Y529F mutant rescues Akt activation. Reduced Src activity correlates with decreased phosphorylation of Gab1, an adapter protein involved in VEGF-dependent Akt activation. Hypophosphorylated Gab1 is unable to fully associate with phosphatidylinositol 3-kinase, VEGFR2, and VE-cadherin complexes, leading to suboptimal Akt activation and increased cell death. Overall, our results reveal that despite its negative role on global VEGFR2 phosphorylation, DEP-1 is a positive regulator of VEGF-mediated Src and Akt activation and endothelial cell survival.
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