ArticleMolecular and cellular biology2003
Dimerization in vivo and inhibition of the nonreceptor form of protein tyrosine phosphatase epsilon.
Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 44 citations in OpenAlex.
- Protein Tyrosine Phosphatase regulation by Reactive Oxygen Species.Advances in cancer research · 2024Review
- The receptor PTPRU is a redox sensitive pseudophosphatase.Nature communications · 2020Article
- RPTPα phosphatase activity is allosterically regulated by the membrane-distal catalytic domain.The Journal of biological chemistry · 2020Article
- Article
- Tuning the Protein Phosphorylation by Receptor Type Protein Tyrosine Phosphatase Epsilon (PTPRE) in Normal and Cancer Cells.Journal of Cancer · 2019Review
- Regulatory Mechanisms and Novel Therapeutic Targeting Strategies for Protein Tyrosine Phosphatases.Chemical reviews · 2018Review
- Proteinaceous Regulators and Inhibitors of Protein Tyrosine Phosphatases.Molecules (Basel, Switzerland) · 2018Review
- The KIM-family protein-tyrosine phosphatases use distinct reversible oxidation intermediates: Intramolecular or intermolecular disulfide bond formation.The Journal of biological chemistry · 2017Article
- Aging is associated with dimerization and inactivation of the brain-enriched tyrosine phosphatase STEP.Neurobiology of aging · 2016Article
- Mining the function of protein tyrosine phosphatases in health and disease.Seminars in cell & developmental biology · 2015Review
- Identification of receptor protein tyrosine phosphatases (RPTPs) as regulators of receptor tyrosine kinases (RTKs) using an RPTP siRNA-RTK substrate screen.Methods in molecular biology (Clifton, N.J.) · 2015Article
- Receptor protein tyrosine phosphatase-receptor tyrosine kinase substrate screen identifies EphA2 as a target for LAR in cell migration.Molecular and cellular biology · 2013Article
- 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
- Oxidative stress-induced oligomerization inhibits the activity of the non-receptor tyrosine phosphatase STEP61.Journal of neurochemistry · 2011Article
- Regulation of apoptotic potassium currents by coordinated zinc-dependent signalling.The Journal of physiology · 2009Article
- Analysis of molecular determinants of PRL-3.Journal of cellular and molecular medicine · 2009Article
- PTPepsilon has a critical role in signaling transduction pathways and phosphoprotein network topology in red cells.Proteomics · 2008Article
- Neu-mediated phosphorylation of protein tyrosine phosphatase epsilon is critical for activation of Src in mammary tumor cells.Oncogene · 2007Article
- 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
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
cyt-PTP epsilon is a naturally occurring nonreceptor form of the receptor-type protein tyrosine phosphatase (PTP) epsilon. As such, cyt-PTP epsilon enables analysis of phosphatase regulation in the absence of extracellular domains, which participate in dimerization and inactivation of the receptor-type phosphatases receptor-type protein tyrosine phosphatase alpha (RPTPalpha) and CD45. Using immunoprecipitation and gel filtration, we show that cyt-PTP epsilon forms dimers and higher-order associations in vivo, the first such demonstration among nonreceptor phosphatases. Although cyt-PTP epsilon readily dimerizes in the absence of exogenous stabilization, dimerization is increased by oxidative stress. Epidermal growth factor receptor stimulation can affect cyt-PTP epsilon dimerization and tyrosine phosphorylation in either direction, suggesting that cell surface receptors can relay extracellular signals to cyt-PTP epsilon, which lacks extracellular domains of its own. The inactive, membrane-distal (D2) phosphatase domain of cyt-PTP epsilon is a major contributor to intermolecular binding and strongly interacts in a homotypic manner; the presence of D2 and the interactions that it mediates inhibit cyt-PTP epsilon activity. Intermolecular binding is inhibited by the extreme C and N termini of D2. cyt-PTP epsilon lacking these regions constitutively dimerizes, and its activities in vitro towards para-nitrophenylphosphate and in vivo towards the Kv2.1 potassium channel are markedly reduced. We conclude that physiological signals can regulate dimerization and phosphorylation of cyt-PTP epsilon in the absence of direct interaction between the PTP and extracellular molecules. Furthermore, dimerization can be mediated by the D2 domain and does not strictly require the presence of PTP extracellular domains.
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