ArticleThe Journal of cell biology1993
Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation.
Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.
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Who cites it
85 citing papers in PubMed, 265 citations in OpenAlex.
- 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
- Role of protein tyrosine phosphatase receptor type M in epithelial ovarian cancer progression.Journal of ovarian research · 2023Article
- Artificial Intelligence-Based Computational Screening and Functional Assays Identify Candidate Small Molecule Antagonists of PTPmu-Dependent Adhesion.International journal of molecular sciences · 2023Article
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- PTPRM Is Critical for Synapse Formation Regulated by Zinc Ion.Frontiers in molecular neuroscience · 2022Article
- Protein tyrosine phosphatases in cell adhesion.The Biochemical journal · 2021Review
- Detection of Tumor-Specific PTPmu in Gynecological Cancer and Patient Derived Xenografts.Diagnostics (Basel, Switzerland) · 2021Article
- A PTPmu Biomarker is Associated with Increased Survival in Gliomas.International journal of molecular sciences · 2019Article
- Article
- Expression of receptor-type protein tyrosine phosphatase in developing and adult renal vasculature.PloS one · 2017Article
- Review
- Loss of PTPRM associates with the pathogenic development of colorectal adenoma-carcinoma sequence.Scientific reports · 2015Article
- Inactivation of the catalytic phosphatase domain of PTPRT/RPTPρ increases social interaction in mice.Autism research : official journal of the International Society for Autism Research · 2015Article
- Regulation of Endothelial Adherens Junctions by Tyrosine Phosphorylation.Mediators of inflammation · 2015Review
- Extracellular regulation of type IIa receptor protein tyrosine phosphatases: mechanistic insights from structural analyses.Seminars in cell & developmental biology · 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
- Osteoblastic protein tyrosine phosphatases inhibition and connexin 43 phosphorylation by alendronate.Experimental cell research · 2014Article
- Receptor-type tyrosine phosphatase ligands: looking for the needle in the haystack.The FEBS journal · 2013Review
25 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
No grant is acknowledged in the PubMed record.
Abstract
The receptor-like protein tyrosine phosphatase, PTPmu, displays structural similarity to cell-cell adhesion molecules of the immunoglobulin superfamily. We have investigated the ability of human PTPmu to function in such a capacity. Expression of PTPmu, with or without the PTPase domains, by recombinant baculovirus infection of Sf9 cells induced their aggregation. However, neither a chimeric form of PTPmu, containing the extracellular and transmembrane segments of the EGF receptor and the intracellular segment of PTPmu, nor the intracellular segment of PTPmu expressed as a soluble protein induced aggregation. PTPmu mediates aggregation via a homophilic mechanism, as judged by lack of incorporation of uninfected Sf9 cells into aggregates of PTPmu-expressing cells. Homophilic binding has been demonstrated between PTPmu-coated fluorescent beads (Covaspheres) and endogenously expressed PTPmu on MvLu cells. Additionally the PTPmu-coated beads specifically bound to a bacterially expressed glutathione-S-transferase fusion protein containing the extracellular segment of PTPmu (GST/PTPmu) adsorbed to petri dishes. Covaspheres coated with the GST/PTPmu fusion protein aggregated in vitro and also bound to PTPmu expressed endogenously on MvLu cells. These results suggest that the ligand for this transmembrane PTPase is another PTPmu molecule on an adjacent cell. Thus homophilic binding interactions may be an important component of the function of PTPmu 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.