ArticleOncogene2007
Neu-mediated phosphorylation of protein tyrosine phosphatase epsilon is critical for activation of Src in mammary tumor cells.
Article in Oncogene, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 37 citations in OpenAlex.
- High-fat diet in a mouse insulin-resistant model induces widespread rewiring of the phosphotyrosine signaling network.Molecular systems biology · 2019Article
- Protein tyrosine phosphatases: promising targets in pancreatic ductal adenocarcinoma.Cellular and molecular life sciences : CMLS · 2019Review
- Tuning the Protein Phosphorylation by Receptor Type Protein Tyrosine Phosphatase Epsilon (PTPRE) in Normal and Cancer Cells.Journal of Cancer · 2019Review
- Adaptor protein GRB2 promotes Src tyrosine kinase activation and podosomal organization by protein-tyrosine phosphatase ϵ in osteoclasts.The Journal of biological chemistry · 2014Article
- Protein tyrosine phosphatases ε and α perform nonredundant roles in osteoclasts.Molecular biology of the cell · 2014Article
- Metabolic regulation by protein tyrosine phosphatases.Journal of biomedical research · 2014Article
- Epidermal growth factor receptor (EGFR)-mediated positive feedback of protein-tyrosine phosphatase epsilon (PTPepsilon) on ERK1/2 and AKT protein pathways is required for survival of human breast cancer cells.The Journal of biological chemistry · 2012Article
- Synapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and Fyn.The EMBO journal · 2009Article
- Protein tyrosine phosphatase epsilon regulates integrin-mediated podosome stability in osteoclasts by activating Src.Molecular biology of the cell · 2009Article
- Association of tyrosine phosphatase epsilon with microtubules inhibits phosphatase activity and is regulated by the epidermal growth factor receptor.Molecular and cellular biology · 2007Article
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
The receptor-type protein tyrosine phosphatase epsilon (RPTPepsilon) activates c-Src in mammary tumor cells induced in vivo by Neu. Tumor cells lacking RPTPepsilon exhibit reduced c-Src activity, appear less transformed morphologically and proliferate slower in vitro and in vivo. Expression of Src rescues most of these phenotypes, indicating that c-Src activity is important for maintaining the transformed phenotype. However, the molecular mechanisms that control activation of c-Src by RPTPepsilon are unknown. We show that Neu induces phosphorylation of RPTPepsilon exclusively at its C-terminal Y695, and that this phosphorylation is required for activation of c-Src by RPTPepsilon. Phosphorylation of RPTPepsilon does not affect its activity toward another substrate, the voltage-gated potassium channel Kv2.1, suggesting that phosphorylation directs RPTPepsilon activity toward c-Src. Phosphorylation of RPTPepsilon reduces its dimerization at the cell membrane, although this does not affect its activity significantly. RPTPepsilon is subject to strong auto- and trans-dephosphorylation, suggesting that dephosphorylation limits the activation of c-Src downstream of Neu. We conclude that an Neu-RPTPepsilon-Src signaling pathway exists in mammary tumor cells, in which phosphorylation of RPTPepsilon by Neu directs RPTPepsilon to activate c-Src. Reversible phosphorylation of RPTPepsilon at Y695 may thus function as a 'molecular switch', which affects the substrate specificity of the phosphatase.
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