Identification of Shp-2 as a Stat5A Phosphatase*
Explore this paper's citation graph
Summary
It is demonstrated that down-regulation of the tyrosine-phosphorylated Stat5A was via deph phosphorylation, and it is concluded that Shp-2 is aStat5A phosphatase, which down-regulates the active Stat 5A in vivo.
- Type
- article
- Published
- 2003-05-09
- Cited by
- 139
- References
- 52
- Access
- Open access
- OpenAlex
- https://openalex.org/W1964480633
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:35311140
Keywords
Dephosphorylation, Phosphorylation, Protein tyrosine phosphatase, Tyrosine, Tyrosine phosphorylation
References
- Shp-2 Tyrosine Phosphatase Functions as a Negative Regulator of the Interferon-Stimulated Jak/STAT Pathway
- Interleukin‐3, granulocyte‐macrophage colony stimulating factor and interleukin‐5 transduce signals through two STAT5 homologs.
- The ubiquitin conjugation system is required for ligand‐induced endocytosis and degradation of the growth hormone receptor.
- Thrombopoietin activates a STAT5‐like factor in hematopoietic cells.
- Prolactin, growth hormone, erythropoietin and granulocyte‐macrophage colony stimulating factor induce MGF‐Stat5 DNA binding activity.
- CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling
- The rapid inactivation of nuclear tyrosine phosphorylated Stat1 depends upon a protein tyrosine phosphatase.
- PTP1D is a positive regulator of the prolactin signal leading to beta‐casein promoter activation.
- Role of accurate mass measurement (+/- 10 ppm) in protein identification strategies employing MS or MS/MS and database searching.
- Cytokine receptor signalling
- A Functional Nuclear Localization Sequence in the C-terminal Domain of SHP-1*
- The Stat family in cytokine signaling.
- JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin.
- The COOH-terminal Tyrosine Phosphorylation Sites on IRS-1 Bind SHP-2 and Negatively Regulate Insulin Signaling*
- Involvement of Protein Phosphatase 2A in the Interleukin-3-Stimulated Jak2-Stat5 Signaling Pathway
- Shp-2 tyrosine phosphatase: signaling one cell or many.
- Specific inhibition of Stat3 signal transduction by PIAS3.
- Combinatorial control of the specificity of protein tyrosine phosphatases.
- The role of shared receptor motifs and common Stat proteins in the generation of cytokine pleiotropy and redundancy by IL-2, IL-4, IL-7, IL-13, and IL-15.
- SOCS proteins, regulators of intracellular signaling.
Cited by
- SHP-2 tyrosine phosphatase in human diseases.
- Regulation of inflammatory signalling in adipocytes by AMPK
- Adenosine Acts through A2 Receptors to Inhibit IL-2-Induced Tyrosine Phosphorylation of STAT5 in T Lymphocytes: Role of Cyclic Adenosine 3′,5′-Monophosphate and Phosphatases1
- Granulocyte colony-stimulating factor and its receptor in normal myeloid cell development, leukemia and related blood cell disorders.
- STUDIES ON THE T CELL SUPPRESSIVE AND ANTI-ANGIOGENIC ACTIVITIES OF THE DIETARY PHYTOCHEMICAL PIPERINE
- Decreased STAT5 phosphorylation and GATA-3 expression in NOX2 deficient T cells: Role in T helper development
- Investigation of the cAMP-mediated inhibitory mechanism on the signalling pathways of 2 cytokines : IL-6 and leptin in endothelial cells
- Interferon signaling in chronic hepatitis C : mechanisms and implications for therapy
- Suppressors Of Cytokine Signaling in G-CSF-induced neutrophil development
- Funktionalität des Interferon TypI- und TypII-Signalwegs in Burkitt-Lymphom-Zellen
- Phosphorylation of Grb2-Associated Binder 2 on Serine 623 by ERK MAPK Regulates Its Association with the Phosphatase SHP-2 and Decreases STAT5 Activation1
- Inhibition of Natural Killer Cell Cytotoxicity by Interleukin‐6: Implications for the Pathogenesis of Macrophage Activation Syndrome
- Inhibition of STAT5: A therapeutic option in BCR-ABL1-driven leukemia
- Molecular mechanisms of FLT3-ITD-induced leukemogenesis
- STATs as critical mediators of signal transduction and transcription: lessons learned from STAT5.
- Receptor and nonreceptor protein tyrosine phosphatases in the nervous system
- The tyrosine phosphatase SHP2 is required for cell transformation by the receptor tyrosine kinase mutants FIP1L1‐PDGFRα and PDGFRα D842V
- Regulation of JAK–STAT signalling in the immune system
- Conditional Deletion of Shp2 in the Mammary Gland Leads to Impaired Lobulo-alveolar Outgrowth and Attenuated Stat5 Activation*
- SHD1 is a novel cytokine-inducible, negative feedback regulator of STAT5-dependent transcription.
Related papers
- Measuring the Activities of Two-Component Regulatory System Phosphatases.
- Dephosphorylation of the deinhibitor protein by the PCSH protein phosphatase
- The protein phosphatases involved in cellular regulation. Identification of the inhibitor-2 phosphatases in rabbit skeletal muscle.
- Dephosphorylation of microtubule-binding sites at the neurofilament-H tail domain by alkaline, acid, and protein phosphatases.
- Dephosphorylation of Cardiac Proteins in vitro - a matter of Phosphatase Specificity
- Two dephosphorylation pathways of inositol 1,4,5-trisphosphate in homogenates of the cellular slime mould Dictyostelium discoideum.
- Modulation of synaptosomal protein phosphorylation/dephosphorylation by calcium is antagonised by inhibition of protein phosphatases with okadaic acid.
- Phosphatase Activity Toward Abnormally Phosphorylated τ: Decrease in Alzheimer Disease Brain