The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP

Pettiford, Sherrie M.; Herbst, Ronald

doi:10.1038/sj.onc.1203408

Cited by 41 publications

(37 citation statements)

References 46 publications

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“…6,7 HePTP is constitutively expressed in K562 cells and overexpression of this PTP interferes with ERK2 activation. 13 To better understand the role of HePTP in ERK regulation and cell differentiation we had previously used a catalytically inactive mutant of HePTP (HePTP-C/S), in which the conserved cystein residue of the PTP active site was replaced with serine, to interfere with the function of endogenous HePTP. In contrast to wild-type HePTP, overexpression of this mutant in K562 cells had no significant effect on PMA-induced tyrosine phosphorylation of ERK1/2.…”

Section: Heptp Antisense Cdna Specifically Reduces Heptp Protein Levementioning

confidence: 99%

“…Transfectants were obtained as described previously. 13 Polyclonal stable lines were established by placing cells under G418 (800 mg/ml) selection 48 h after transfection with continued growth under selection for 5 weeks prior to analysis. Clonal lines were established by serial dilution in 96-well plates.…”

Section: Cells and Transfectionsmentioning

confidence: 99%

“…In the present report, we have studied the effect of HePTP on megakaryocytic differentiation of K562 cells which constitutively express this phosphatase 13 . As outlined above, proliferation and differentiation of K562 cells is largely determined by the magnitude and duration of ERK activity.…”

Section: Introductionmentioning

confidence: 99%

“…The KIM sequence is required for association with and dephosphorylation of active ERK1/2. [11][12][13]15,20 Within this sequence is a consensus site for phosphorylation by cAMP-dependent protein kinase (PKA). It was recently demonstrated that phosphorylation of this site in PTP-SL and HePTP in response to PKA activation inhibits the interaction of these phosphatases with their substrates and, consequently, results in increased ERK activity.…”

Section: Introductionmentioning

confidence: 99%

“…More recently, the tyrosine-specific protein phosphatase (PTP) HePTP (also known as LC-PTP) was identified as an ERK1/2 phosphatase. [11][12][13] For example, overexpression of HePTP in Jurkat T cells blocks ERK1/2 activation after engagement of the T cell receptor and overexpression in K562 cells interferes with the activation of ERK1/2 in response to PMA. 11,13,14 In T cells, HePTP also binds and dephosphorylates the MAP-kinase family member p38 while in K562 cells ERK2 is the predominant substrate.…”

Section: Introductionmentioning

confidence: 99%

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The protein tyrosine phosphatase HePTP regulates nuclear translocation of ERK2 and can modulate megakaryocytic differentiation of K562 cells

Pettiford¹,

Herbst²

2003

Leukemia

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Section: Heptp Antisense Cdna Specifically Reduces Heptp Protein Levementioning

confidence: 99%

Section: Cells and Transfectionsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

The protein tyrosine phosphatase HePTP regulates nuclear translocation of ERK2 and can modulate megakaryocytic differentiation of K562 cells

Pettiford¹,

Herbst²

2003

Leukemia

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PTPN7 mediates macrophage‐polarization and determines immunotherapy in gliomas: A single‐cell sequencing analysis

Ji,

Cheng,

et al. 2024

Environmental Toxicology

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BackgroundProtein tyrosine phosphatase non‐receptor type 7 (PTPN7) is a signaling molecule that regulates a multitude of cellular processes, spanning cell proliferation, cellular differentiation, the mitotic cycle, and oncogenic metamorphosis. However, the characteristic of PTPN7 in the glioma microenvironment has yet to be elucidated.MethodsThe prognostic value, genomic features, immune characteristics, chemotherapy prediction, and immunotherapy prediction of PTPN7 were systematically explored at the bulk sequencing level. The cell evolution trajectory, cell communication pattern, and cell metabolic activity related to PTPN7 were systematically explored at the single‐cell sequencing level. HMC3 and M0 cells were cocultured with U251 and T98G cells, and flow cytometry was carried out to investigate the polarization of HMC3 and M0. Transwell assay and CCK‐8 assay were performed to explore the migration and proliferation activity of U251 and T98G.ResultsThe expression level of PTPN7 is significantly elevated in glioma and indicates malignant features. PTPN7 expression predicts worse prognosis of glioma patients. PTPN7 is associated with genome alteration and immune infiltration. Besides, PTPN7 plays a crucial role in modulating metabolic and immunogenic processes, particularly by influencing the activity of microglia and macrophages through multiple signaling pathways involved in cellular communication. Specifically, PTPN7 actively mediates inflammation‐resolving‐polarization of macrophages and microglia and protects glioma from immune attack. PTPN7 could also predict the response of immunotherapy.ConclusionsPTPN7 is critically involved in inflammation‐resolving‐polarization mediated by macrophage and microglia and promotes the immune escape of glioma cells.

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Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for map kinase regulation 1 1Edited by D. Rees

Szedlacsek

Aricescu

Fulga

et al. 2001

Journal of Molecular Biology

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The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP

Cited by 41 publications

References 46 publications

The protein tyrosine phosphatase HePTP regulates nuclear translocation of ERK2 and can modulate megakaryocytic differentiation of K562 cells

The protein tyrosine phosphatase HePTP regulates nuclear translocation of ERK2 and can modulate megakaryocytic differentiation of K562 cells

PTPN7 mediates macrophage‐polarization and determines immunotherapy in gliomas: A single‐cell sequencing analysis

Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for map kinase regulation 1 1Edited by D. Rees

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