ArticleThe Journal of cell biology1995
Receptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivo.
Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
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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.
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Who cites it
80 citing papers in PubMed, 308 citations in OpenAlex.
- Nucleic acid spheres for treating capillarisation of liver sinusoidal endothelial cells in liver fibrosis.Nature communications · 2025Article
- A novel binding pocket in the D2 domain of protein tyrosine phosphatase mu (PTPmu) guides AI screen to identify small molecules that modulate tumour cell adhesion, growth and migration.Journal of cellular and molecular medicine · 2023Article
- Article
- Finding New Ways How to Control BACE1.The Journal of membrane biology · 2022Article
- Host-microbiome protein-protein interactions capture disease-relevant pathways.Genome biology · 2022Article
- Effect of Cadherin-11 Expression on the Prognosis of a Newly Diagnosed Primary Glioblastoma.Brain tumor research and treatment · 2021Article
- A genome-wide association study on medulloblastoma.Journal of neuro-oncology · 2020Article
- Prolonged Exposure to Insulin Inactivates Akt and ErkJournal of the Endocrine Society · 2019Article
- A central role for cadherin signaling in cancer.Experimental cell research · 2017Review
- Brain Region and Isoform-Specific Phosphorylation Alters Kalirin SH2 Domain Interaction Sites and Calpain Sensitivity.ACS chemical neuroscience · 2017Article
- Biophysical Tools to Study Cellular Mechanotransduction.Bioengineering (Basel, Switzerland) · 2017Review
- Expression of receptor-type protein tyrosine phosphatase in developing and adult renal vasculature.PloS one · 2017Article
- Phosphoregulation of the C. elegans cadherin-catenin complex.The Biochemical journal · 2015Article
- Regulation of Endothelial Adherens Junctions by Tyrosine Phosphorylation.Mediators of inflammation · 2015Review
- Regulation of development and cancer by the R2B subfamily of RPTPs and the implications of proteolysis.Seminars in cell & developmental biology · 2015Review
- A protease storm cleaves a cell-cell adhesion molecule in cancer: multiple proteases converge to regulate PTPmu in glioma cells.Journal of cellular biochemistry · 2014Article
- Similarities and differences in the regulation of leukocyte extravasation and vascular permeability.Seminars in immunopathology · 2014Review
- Phosphatase regulation of intercellular junctions.Tissue barriers · 2013Review
- Protein tyrosine phosphatases--from housekeeping enzymes to master regulators of signal transduction.The FEBS journal · 2013Review
- Cadherin-dependent mechanotransduction depends on ligand identity but not affinity.Journal of cell science · 2012Article
20 more citing papers are in PubMed but not listed here.
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 extracellular segment of the receptor-type type protein tyrosine phosphatase PTPmu, possesses an MAM domain, an immunoglobulin domain, and four fibronectin type-III repeats. It binds homophilically, i.e., PTPmu on the surface of one cell binds to PTPmu on an apposing cell, and the binding site lies within the immunoglobulin domain. The intracellular segment of PTPmu has two PTP domains and a juxtamembrane segment that is homologous to the conserved intracellular domain of the cadherins. In cadherins, this segment interacts with proteins termed catenins to mediate association with the actin cytoskeleton. In this article, we demonstrate that PTPmu associates with a complex containing cadherins, alpha- and beta-catenin in mink lung (MvLu) cells, and in rat heart, lung, and brain tissues. Greater than 80% of the cadherin in the cell is cleared from Triton X-100 lysates of MvLu cells after immunoprecipitation with antibodies to PTPmu; however, the complex is dissociated when lysates are prepared in more stringent, SDS-containing RIPA buffer. In vitro binding studies demonstrated that the intracellular segment of PTPmu binds directly to the intracellular domain of E-cadherin, but not to alpha- or beta-catenin. Consistent with their ability to interact in vivo, PTPmu, cadherins, and catenins all localized to points of cell-cell contact in MvLu cells, as assessed by immunocytochemical staining. After pervanadate treatment of MvLu cells, which inhibits cellular tyrosine phosphatase activity including PTPmu, the cadherins associated with PTPmu are now found in a tyrosine-phosphorylated form, indicating that the cadherins may be an endogenous substrate for PTPmu. These data suggest that PTPmu may be one of the enzymes that regulates the dynamic tyrosine phosphorylation, and thus function, of the cadherin/catenin complex in vivo.
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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.