ArticleMolecular and cellular biology2003
A unique autophosphorylation site on Tie2/Tek mediates Dok-R phosphotyrosine binding domain binding and function.
Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
30 citing papers in PubMed, 85 citations in OpenAlex.
- Review
- Decoding infantile hemangioma: cellular dynamics, molecular signals, and microenvironmental influences.Frontiers in oncology · 2025Review
- Anti-angiogenesis in colorectal cancer therapy.Cancer science · 2024Review
- A novel implant surface modification mode of Fe3O4-containing TiO2 nanorods with sinusoidal electromagnetic field for osteoblastogenesis and angiogenesis.Materials today. Bio · 2023Article
- Physiological and pathophysiological mechanisms of the molecular and cellular biology of angiogenesis and inflammation in moyamoya angiopathy and related vascular diseases.Frontiers in neurology · 2023Review
- Novel Drugs with High Efficacy against Tumor Angiogenesis.International journal of molecular sciences · 2022Review
- Endothelial Dysfunction after Hematopoietic Stem Cell Transplantation: A Review Based on Physiopathology.Journal of clinical medicine · 2022Review
- Introduction to DOK2 and its potential role in cancer.Physiological research · 2021Review
- Review
- Adaptor Protein ShcD/Molecular cancer research : MCR · 2021Article
- Cerebral Plasmodium falciparum malaria: The role of PfEMP1 in its pathogenesis and immunity, and PfEMP1-based vaccines to prevent it.Immunological reviews · 2020Review
- Context-dependent functions of angiopoietin 2 are determined by the endothelial phosphatase VEPTP.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A Review of Anti-Angiogenic Targets for Monoclonal Antibody Cancer Therapy.International journal of molecular sciences · 2017Review
- Angiopoietin-2/angiopoietin-1 as non-invasive biomarker of cirrhosis in chronic hepatitis C.World journal of gastroenterology · 2016Article
- Vascular dysfunction as a target for adjuvant therapy in cerebral malaria.Memorias do Instituto Oswaldo Cruz · 2014Review
- The RNA binding protein hnRNP-K mediates post-transcriptional regulation of uncoupling protein-2 by angiopoietin-1.Cellular signalling · 2014Article
- Tie2 and Eph receptor tyrosine kinase activation and signaling.Cold Spring Harbor perspectives in biology · 2014Review
- Tie1 deletion inhibits tumor growth and improves angiopoietin antagonist therapy.The Journal of clinical investigation · 2014Article
- Signaling pathways in the development of infantile hemangioma.Journal of hematology & oncology · 2014Review
- Regulation of angiopoietin-1/Tie-2 receptor signaling in endothelial cells by dual-specificity phosphatases 1, 4, and 5.Journal of the American Heart Association · 2013Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tie2/Tek is an endothelial cell receptor tyrosine kinase that induces signal transduction pathways involved in cell migration upon angiopoietin-1 (Ang1) stimulation. To address the importance of the various tyrosine residues of Tie2 in signal transduction, we generated a series of Tie2 mutants and examined their signaling properties. Using this approach in conjunction with a phosphorylation state-specific antibody, we identified tyrosine residue 1106 on Tie2 as an Ang1-dependent autophosphorylation site that mediates binding and phosphorylation of the downstream-of-kinase-related (Dok-R) docking protein. This tyrosine residue is contained within a unique interaction motif for the phosphotyrosine binding domain of Dok-R, and the pleckstrin homology domain of Dok-R further contributes to Tie2 binding in a phosphatidylinositol 3'-kinase-dependent manner. Introduction of a Tie2 mutant lacking tyrosine residue 1106 into endothelial cells interferes with Dok-R phosphorylation in response to Ang1. Furthermore, this mutant is unable to restore the migration potential of endothelial cells derived from mice lacking Tie2. Together, these findings demonstrate that tyrosine residue 1106 on Tie2 is critical for coupling downstream cell migration signal transduction pathways with Ang1 stimulation in endothelial cells.
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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.