ArticleHistochemistry and cell biology2009
Oligomerized Tie2 localizes to clathrin-coated pits in response to angiopoietin-1.
Article in Histochemistry and cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 19 citations in OpenAlex.
- Angiopoietins: multifaceted mediators in the pathogenesis of joint-related disorders.Histochemistry and cell biology · 2025Review
- Heterogeneity in VEGF Receptor-2 Mobility and Organization on the Endothelial Cell Surface Leads to Diverse Models of Activation by VEGF.Cell reports · 2020Article
- Review
- The role of caveolin-1 in tumors of the brain - functional and clinical implications.Cellular oncology (Dordrecht, Netherlands) · 2019Review
- Overview of Crosstalk Between Multiple Factor of Transcytosis in Blood Brain Barrier.Frontiers in neuroscience · 2019Review
- Review
- TIE2 Associates with Caveolae and Regulates Caveolin-1 To Promote Their Nuclear Translocation.Molecular and cellular biology · 2017Article
- Structural basis of Tie2 activation and Tie2/Tie1 heterodimerization.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Dimerization of Tie2 mediated by its membrane-proximal FNIII domains.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Application of Hanging Drop Technique for Kidney Tissue Culture.Kidney & blood pressure research · 2017Article
- Ligand-independent Tie2 dimers mediate kinase activity stimulated by high dose angiopoietin-1.The Journal of biological chemistry · 2013Article
- Endocytosis of receptor tyrosine kinases.Cold Spring Harbor perspectives in biology · 2013Review
- Extending the knowledge in histochemistry and cell biology.Histochemistry and cell biology · 2010Review
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tyrosine kinase receptor Tie2 is expressed on endothelial cells, and together with its ligand angiopoietin-1 (Ang1), is important for angiogenesis and vascular stability. Upon activation by Ang1, Tie2 is rapidly internalized and degraded, a mechanism most likely necessary to attenuate receptor activity. Using immunogold electron microscopy, we show that on the surface of endothelial cells, Tie2 is arranged in variably sized clusters containing dimers and higher order oligomers. Clusters of Tie2 were expressed on the apical and basolateral plasma membranes, and on the tips of microvilli. Upon activation by Ang1, Tie2 co-localized with the clathrin heavy chain at the apical and basolateral plasma membranes and within endothelial cells indicating that Tie2 internalizes through clathrin-coated pits. Inhibiting cellular endocytosis by depleting cellular potassium or by acidifying the cytosol blocked the internalization of Tie2 in response to Ang1. Our results suggest that one pathway mediating the internalization of Tie2 in response to Ang1 is through clathrin-coated pits.
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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.