ArticleThe Journal of biological chemistry2008
Regulation of the Met receptor-tyrosine kinase by the protein-tyrosine phosphatase 1B and T-cell phosphatase.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
57 citing papers in PubMed, 95 citations in OpenAlex.
- Rational design of a protein-protein interaction inhibitor that activates Protein Tyrosine Phosphatase 1B.bioRxiv : the preprint server for biology · 2026Article
- WTAP-mediated mHuman cell · 2025Article
- Uncovering the individual immunotherapeutic roles of PTPN1 and PTPN2 in T cells during dual inhibition.iScience · 2025Article
- The MET Oncogene: An Update on Targeting Strategies.Pharmaceuticals (Basel, Switzerland) · 2024Review
- An mTOR feedback loop mediates the 'flare' ('rebound') response to MET tyrosine kinase inhibition.Scientific reports · 2023Article
- Catechol-O-methyl transferase suppresses cell invasion and interplays with MET signaling in estrogen dependent breast cancer.Scientific reports · 2023Article
- Ptpn1 deletion protects oval cells against lipoapoptosis by favoring lipid droplet formation and dynamics.Cell death and differentiation · 2022Article
- A systems genomics approach to uncover patient-specific pathogenic pathways and proteins in ulcerative colitis.Nature communications · 2022Article
- Tyrosine phosphatases regulate resistance to ALK inhibitors in ALK+ anaplastic large cell lymphoma.Blood · 2022Article
- Novel function of THEMIS2 in the enhancement of cancer stemness and chemoresistance by releasing PTP1B from MET.Oncogene · 2022Article
- The catalytic activity of TCPTP is auto-regulated by its intrinsically disordered tail and activated by Integrin alpha-1.Nature communications · 2022Article
- The hepatocyte growth factor/mesenchymal epithelial transition factor axis in high-risk pediatric solid tumors and the anti-tumor activity of targeted therapeutic agents.Frontiers in pediatrics · 2022Review
- PD-L1 positively regulates MET phosphorylation through inhibiting PTP1B.Cancer science · 2021Article
- CAPN1 promotes malignant behavior and erlotinib resistance mediated by phosphorylation of c-Met and PIK3R2 via degrading PTPN1 in lung adenocarcinoma.Thoracic cancer · 2020Article
- MET targeting: time for a rematch.Oncogene · 2020Review
- The Landscape of Somatic Copy Number Alterations in Head and Neck Squamous Cell Carcinoma.Frontiers in oncology · 2020Article
- Article
- ER morphology and endo-lysosomal crosstalk: Functions and disease implications.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020Review
- The role of T-cell protein tyrosine phosphatase in epithelial carcinogenesis.Molecular carcinogenesis · 2019Review
- Clinical and biological features of PTPN2-deleted adult and pediatric T-cell acute lymphoblastic leukemia.Blood advances · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The non-receptor protein-tyrosine phosphatases (PTPs) 1B and T-cell phosphatase (TCPTP) have been implicated as negative regulators of multiple signaling pathways including receptor-tyrosine kinases. We have identified PTP1B and TCPTP as negative regulators of the hepatocyte growth factor receptor, the Met receptor-tyrosine kinase. In vivo, loss of PTP1B or TCPTP enhances hepatocyte growth factor-mediated phosphorylation of Met. Using substrate trapping mutants of PTP1B or TCPTP, we have demonstrated that both phosphatases interact with Met and that these interactions require phosphorylation of twin tyrosines (Tyr-1234/1235) in the activation loop of the Met kinase domain. Using confocal microscopy, we show that trapping mutants of both PTP1B and the endoplasmic reticulum-targeted TCPTP isoform, TC48, colocalize with Met and that activation of Met enables the nuclear-localized isoform of TCPTP, TC45, to exit the nucleus. Using small interfering RNA against PTP1B and TCPTP, we demonstrate that phosphorylation of Tyr-1234/1235 in the activation loop of the Met receptor is elevated in the absence of either PTP1B or TCPTP and further elevated upon loss of both phosphatases. This enhanced phosphorylation of Met corresponds to enhanced biological activity and cellular invasion. Our data demonstrate that PTP1B and TCPTP play distinct and non-redundant roles in the regulation of the Met receptor-tyrosine kinase.
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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.