ArticleBiophysical journal2012
Computational analysis of the regulation of EGFR by protein tyrosine phosphatases.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 37 citations in OpenAlex.
- Systems-level consequences of low RAF abundance for EGFR-ERK signaling.Biophysical journal · 2026Article
- Systems Biology of the Cancer Cell.Annual review of biomedical engineering · 2025Review
- Evaluation of information flows in the RAS-MAPK system using transfer entropy measurements.eLife · 2025Article
- Mathematical Modeling and Inference of Epidermal Growth Factor-Induced Mitogen-Activated Protein Kinase Cell Signaling Pathways.International journal of molecular sciences · 2024Review
- Ten Approaches That Improve Immunostaining: A Review of the Latest Advances for the Optimization of Immunofluorescence.International journal of molecular sciences · 2022Review
- Exendin-4 restores airway mucus homeostasis through the GLP1R-PKA-PPARγ-FOXA2-phosphatase signaling.Mucosal immunology · 2020Article
- Disrupting the transmembrane domain-mediated oligomerization of protein tyrosine phosphatase receptor J inhibits EGFR-driven cancer cell phenotypes.The Journal of biological chemistry · 2019Article
- GP78 Cooperates with Dual-Specificity Phosphatase 1 To Stimulate Epidermal Growth Factor Receptor-Mediated Extracellular Signal-Regulated Kinase Signaling.Molecular and cellular biology · 2019Article
- A conformational sensor based on genetic code expansion reveals an autocatalytic component in EGFR activation.Nature communications · 2018Article
- Phosphatases control PKA-dependent functional microdomains at the outer mitochondrial membrane.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- CyclicOncotarget · 2018Article
- An engineering design approach to systems biology.Integrative biology : quantitative biosciences from nano to macro · 2017Review
- PTPRO represses ERBB2-driven breast oncogenesis by dephosphorylation and endosomal internalization of ERBB2.Oncogene · 2017Article
- Cell signaling regulation by protein phosphorylation: a multivariate, heterogeneous, and context-dependent process.Current opinion in biotechnology · 2016Review
- Review
- Quantitative analysis reveals how EGFR activation and downregulation are coupled in normal but not in cancer cells.Nature communications · 2015Article
- The AXL Receptor is a Sensor of Ligand Spatial Heterogeneity.Cell systems · 2015Article
- Single Particle Tracking Reveals that EGFR Signaling Activity Is Amplified in Clathrin-Coated Pits.PloS one · 2015Article
- Identifying Determinants of EGFR-Targeted Therapeutic Biochemical Efficacy Using Computational Modeling.CPT: pharmacometrics & systems pharmacology · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The tyrosine phosphorylated epidermal growth factor receptor (EGFR) initiates numerous cell signaling pathways. Although EGFR phosphorylation levels are ultimately determined by the balance of receptor kinase and protein tyrosine phosphatase (PTP) activities, the kinetics of EGFR dephosphorylation are not well understood. Previous models of EGFR signaling have generally neglected PTP activity or computed PTP activity by considering data that do not fully reveal the kinetics and compartmentalization of EGFR dephosphorylation. We developed a compartmentalized, mechanistic model to elucidate the kinetics of EGFR dephosphorylation and the coupling of this process to phosphorylation-dependent EGFR endocytosis. Model regression against data from HeLa cells for EGFR phosphorylation response to EGFR activation, PTP inhibition, and EGFR kinase inhibition led to the conclusion that EGFR dephosphorylation occurs at the plasma membrane and in the cell interior with a timescale that is smaller than that for ligand-mediated EGFR endocytosis. The model further predicted that sufficiently rapid dephosphorylation of EGFR at the plasma membrane could potentially impede EGFR endocytosis, consistent with recent experimental findings. Overall, our results suggest that PTPs regulate multiple receptor-level phenomena via their action at the plasma membrane and cell interior and point to new possibilities for targeting PTPs for modulation of EGFR dynamics.
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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.