ArticlePloS one2014
Dynamic recruitment of protein tyrosine phosphatase PTPD1 to EGF stimulation sites potentiates EGFR activation.
Article in PloS one, 2014. 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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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- The role of classical protein tyrosine phosphatases in diabetic kidney disease and therapeutic implications.Journal of biomedical science · 2026Review
- Genome-wide CRISPR screens identify PTPN21 and WDR26 as modulators of the mitochondrial stress-induced ISR.Life metabolism · 2024Article
- Structural analysis of the FERM domain of human protein tyrosine phosphatase non-receptor type 21.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Structural analysis of PTPN21 reveals a dominant-negative effect of the FERM domain on its phosphatase activity.Science advances · 2024Article
- Use of Fluorescence Recovery After Photobleaching (FRAP) to Measure In Vivo Dynamics of Cell Junction-Associated Polarity Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Molecular Analysis of the Interaction between Human PTPN21 and the Oncoprotein E7 from Human Papillomavirus Genotype 18.Molecules and cells · 2021Article
- Review
- Fast Diffusion Sustains Plasma Membrane Accumulation of Phosphatase of Regenerating Liver-1.Frontiers in cell and developmental biology · 2020Article
- PTPN21 and Hook3 relieve KIF1C autoinhibition and activate intracellular transport.Nature communications · 2019Article
- Going Too Far Is the Same as Falling ShortFrontiers in cellular neuroscience · 2019Review
- Interdependence between EGFR and Phosphatases Spatially Established by Vesicular Dynamics Generates a Growth Factor Sensing and Responding Network.Cell systems · 2018Article
- Defining the Protein-Protein Interaction Network of the Human Protein Tyrosine Phosphatase Family.Molecular & cellular proteomics : MCP · 2016Article
- Quantitative analysis reveals how EGFR activation and downregulation are coupled in normal but not in cancer cells.Nature communications · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Balanced activity of protein tyrosine kinases and phosphatases (PTPs) controls tyrosine phosphorylation levels and, consequently, is needed to prevent pathologies like cancer. Phosphatase activity is tightly regulated in space and time. Thus, in order to understand how phospho-tyrosine signalling is regulated, the intracellular dynamics of PTPs should be investigated. Here, we have studied the intracellular dynamics of PTPD1, a FERM (four-point-one, ezrin, radixin, moesin) domain-containing PTP that is over expressed in cancer cells and potentiates EGFR signalling. Whereas PTPD1 was excluded from E-cadherin rich cell-cell adhesions in epithelial cell monolayers, it diffused from the cytoplasm to those membranes in contact with the extracellular medium. Localisation of PTPD1 at the plasma membrane was mediated by its FERM domain and enabled the formation of EGFR/PTPD1-containing signalling complexes that pre-existed at the plasma membrane before EGF stimulation. PTPD1 and EGFR transiently co-localised at EGF stimulation sites until the formation of macropinosomes containing active species of EGFR. Interference of PTPD1 expression caused a decrease in EGFR phosphorylated species at the periphery of the cell. Presented data suggest that the transient formation of dynamic PTPD1/EGFR signalling complexes strengthens EGF signalling by promoting the spatial propagation of EGFR phosphorylated species.
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