ArticlePloS one2012
Regulation of signaling at regions of cell-cell contact by endoplasmic reticulum-bound protein-tyrosine phosphatase 1B.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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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.
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
35 citing papers in PubMed, 58 citations in OpenAlex.
- Mapping of PTP1B, TCPTP, SHP2, and Putative Substrates Reveals Novel Networks in Glomerular Podocytes.Journal of cellular physiology · 2026Article
- CEP hormones at the nexus of nutrient acquisition and allocation, root development, and plant-microbe interactions.Journal of experimental botany · 2024Review
- Protein tyrosine phosphatase 1B is a regulator of alpha-actinin4 in the glomerular podocyte.Biochimica et biophysica acta. Molecular cell research · 2024Article
- The EGFR phosphatase RPTPγ is a redox-regulated suppressor of promigratory signaling.The EMBO journal · 2023Article
- Article
- Structural and functional analysis of tomato sterol C22 desaturase.BMC plant biology · 2021Article
- l-Lactate Dehydrogenase Identified as a Protein Tyrosine Phosphatase 1B Substrate by Using K-BIPS.Chembiochem : a European journal of chemical biology · 2021Article
- The functional universe of membrane contact sites.Nature reviews. Molecular cell biology · 2020Review
- Sticking With It: ER-PM Membrane Contact Sites as a Coordinating Nexus for Regulating Lipids and Proteins at the Cell Cortex.Frontiers in cell and developmental biology · 2020Review
- Lipids or Proteins: Who Is Leading the Dance at Membrane Contact Sites?Frontiers in plant science · 2019Review
- Quantification of protein mobility and associated reshuffling of cytoplasm during chemical fixation.Scientific reports · 2018Article
- Annexins-Coordinators of Cholesterol Homeostasis in Endocytic Pathways.International journal of molecular sciences · 2018Review
- The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures.Communications biology · 2018Article
- Identification and Characterization of Sterol Acyltransferases Responsible for Steryl Ester Biosynthesis in Tomato.Frontiers in plant science · 2018Article
- Phospho-Regulation of Soma-to-Axon Transcytosis of Neurotrophin Receptors.Developmental cell · 2017Article
- Small extracellular vesicles secreted from senescent cells promote cancer cell proliferation through EphA2.Nature communications · 2017Article
- S-nitrosylation of endogenous protein tyrosine phosphatases in endothelial insulin signaling.Free radical biology & medicine · 2016Article
- Endoplasmic reticulum-plasma membrane junctions: structure, function and dynamics.The Journal of physiology · 2016Review
- PTP1B triggers integrin-mediated repression of myosin activity and modulates cell contractility.Biology open · 2015Article
- Ubiquitination switches EphA2 vesicular traffic from a continuous safeguard to a finite signalling mode.Nature communications · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 5 institutions in 3 countries.
Funding
Abstract
Protein-tyrosine phosphatase 1B (PTP1B) is a ubiquitously expressed PTP that is anchored to the endoplasmic reticulum (ER). PTP1B dephosphorylates activated receptor tyrosine kinases after endocytosis, as they transit past the ER. However, PTP1B also can access some plasma membrane (PM)-bound substrates at points of cell-cell contact. To explore how PTP1B interacts with such substrates, we utilized quantitative cellular imaging approaches and mathematical modeling of protein mobility. We find that the ER network comes in close proximity to the PM at apparently specialized regions of cell-cell contact, enabling PTP1B to engage substrate(s) at these sites. Studies using PTP1B mutants show that the ER anchor plays an important role in restricting its interactions with PM substrates mainly to regions of cell-cell contact. In addition, treatment with PTP1B inhibitor leads to increased tyrosine phosphorylation of EphA2, a PTP1B substrate, specifically at regions of cell-cell contact. Collectively, our results identify PM-proximal sub-regions of the ER as important sites of cellular signaling regulation by PTP1B.
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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.