ArticlePloS one2016
Constitutive Association of Tie1 and Tie2 with Endothelial Integrins is Functionally Modulated by Angiopoietin-1 and Fibronectin.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 39 citations in OpenAlex.
- Review
- Insights to Ang/Tie signaling pathway: another rosy dawn for treating retinal and choroidal vascular diseases.Journal of translational medicine · 2024Review
- Therapeutic Strategies for Angiogenesis Based on Endothelial Cell Epigenetics.Journal of cardiovascular translational research · 2024Review
- Construction of an Exudative Age-Related Macular Degeneration Diagnostic and Therapeutic Molecular Network Using Multi-Layer Network Analysis, a Fuzzy Logic Model, and Deep Learning Techniques: Are Retinal and Brain Neurodegenerative Disorders Related?Pharmaceuticals (Basel, Switzerland) · 2023Article
- Rebastinib attenuates liver injury following cecal ligation and puncture in male mice.Journal of medicine and life · 2023Article
- Polydom/SVEP1 binds to Tie1 and promotes migration of lymphatic endothelial cells.The Journal of cell biology · 2023Article
- Article
- Advances in neovascularization after diabetic ischemia.World journal of diabetes · 2022Review
- Mechanical regulation of signal transduction in angiogenesis.Frontiers in cell and developmental biology · 2022Review
- F-domain valency determines outcome of signaling through the angiopoietin pathway.EMBO reports · 2021Article
- A systems biology model of junctional localization and downstream signaling of the Ang-Tie signaling pathway.NPJ systems biology and applications · 2021Article
- F-domain valency determines outcome of signaling through the angiopoietin pathway.bioRxiv : the preprint server for biology · 2020Article
- ΔNp73/ETS2 complex drives glioblastoma pathogenesis- targeting downstream mediators by rebastinib prolongs survival in preclinical models of glioblastoma.Neuro-oncology · 2020Article
- Imaging of Tie2 with a Fluorescently Labeled Small Molecule Affinity Ligand.ACS chemical biology · 2020Article
- Polarization and sprouting of endothelial cells by angiopoietin-1 require PAK2 and paxillin-dependent Cdc42 activation.Molecular biology of the cell · 2019Article
- Intravitreal AAV2.COMP-Ang1 Attenuates Deep Capillary Plexus Expansion in the Aged Diabetic Mouse Retina.Investigative ophthalmology & visual science · 2019Article
- Review
- A collagen IV-derived peptide disrupts α5β1 integrin and potentiates Ang2/Tie2 signaling.JCI insight · 2019Article
- Targeting the Tie2-αBMC biology · 2018Article
- Chemotherapy-induced metastasis: mechanisms and translational opportunities.Clinical & experimental metastasis · 2018Review
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Functional cross-talk between Tie2 and Integrin signaling pathways is essential to coordinate endothelial cell adhesion and migration in response to the extracellular matrix, yet the mechanisms behind this phenomenon are unclear. Here, we examine the possibility that receptor cross-talk is driven through uncharacterized Tie-integrin interactions on the endothelial surface. Using a live cell FRET-based proximity assay, we monitor Tie-integrin receptor recognition and demonstrate that both Tie1 and Tie2 readily associate with integrins α5ß1 and αVß3 through their respective ectodomains. Although not required, Tie2-integrin association is significantly enhanced in the presence of the extracellular component and integrin ligand fibronectin. In vitro binding assays with purified components reveal that Tie-integrin recognition is direct, and further demonstrate that the receptor binding domain of the Tie2 ligand Ang-1, but not the receptor binding domain of Ang-2, can independently associate with α5ß1 or αVß3. Finally, we reveal that cooperative Tie/integrin interactions selectively stimulate ERK/MAPK signaling in the presence of both Ang-1 and fibronectin, suggesting a molecular mechanism to sensitize Tie2 to extracellular matrix. We provide a mechanistic model highlighting the role of receptor localization and association in regulating distinct signaling cascades and in turn, the angiogenic switch.
Indexed as
Identifiers
What OpenQuestion holds
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.