ArticleThe Journal of biological chemistry2010
Protein phosphatase 2A regulates interleukin-2 receptor complex formation and JAK3/STAT5 activation.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
25 citing papers in PubMed, 38 citations in OpenAlex.
- Data Mining for Identification of Targets and Repurposed Drugs to Eliminate Persistent Chronic Myeloid Leukaemia Stem Cells: Targeting RAS/RAF Signalling.Oncology research · 2026Article
- JAK/STAT in human diseases: a common axis in immunodeficiencies and hematological disorders.Frontiers in immunology · 2025Review
- Protein Phosphatase 2A: Role in T Cells and Diseases.Journal of immunology research · 2023Review
- Review
- Phosphorylation of CrkL S114 induced by common gamma chain cytokines and T-cell receptor signal transduction.Scientific reports · 2021Article
- Proteasome α6 Subunit Negatively Regulates the JAK/STAT Pathway and Blood Cell Activation inFrontiers in immunology · 2021Article
- PP2A and tumor radiotherapy.Hereditas · 2020Review
- CD25 and Protein Phosphatase 2A Cooperate to Enhance IL-2R Signaling in Human Regulatory T Cells.Journal of immunology (Baltimore, Md. : 1950) · 2019Article
- Modulation of MutantMolecular cancer research : MCR · 2019Article
- Ten years of research on the role of BVES/ POPDC1 in human disease: a review.OncoTargets and therapy · 2019Review
- Inhibitors of the PI3K/mTOR pathway prevent STAT5 phosphorylation inOncotarget · 2017Article
- Article
- PROTOCADHERIN 7 Acts through SET and PP2A to Potentiate MAPK Signaling by EGFR and KRAS during Lung Tumorigenesis.Cancer research · 2017Article
- Effects of Di-(2-ethylhexyl) Phthalate on Lipid Metabolism by the JAK/STAT Pathway in Rats.International journal of environmental research and public health · 2016Article
- Low-Dose IL-2 in the Treatment of Lupus.Current rheumatology reports · 2016Review
- Promoting Immune Regulation in Type 1 Diabetes Using Low-Dose Interleukin-2.Current diabetes reports · 2016Review
- Interleukin-2 Receptor β Thr-450 Phosphorylation Is a Positive Regulator for Receptor Complex Stability and Activation of Signaling Molecules.The Journal of biological chemistry · 2015Article
- Therapeutic window of interleukin-2 for autoimmune diseases.Diabetes · 2015Article
- LB100, a small molecule inhibitor of PP2A with potent chemo- and radio-sensitizing potential.Cancer biology & therapy · 2015Review
- Protein phosphatase 2A: a target for anticancer therapy.The Lancet. Oncology · 2013Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Reversible protein phosphorylation plays a key role in interleukin-2 (IL-2) receptor-mediated activation of Janus tyrosine kinase 3 (JAK3) and signal transducer and activator of transcription 5 (STAT5) in lymphocytes. Although the mechanisms governing IL-2-induced tyrosine phosphorylation and activation of JAK3/STAT5 have been extensively studied, the role of serine/threonine phosphorylation in controlling these effectors remains to be elucidated. Using phosphoamino acid analysis, JAK3 and STAT5 were determined to be serine and tyrosine-phosphorylated in response to IL-2 stimulation of the human natural killer-like cell line, YT. IL-2 stimulation also induced serine/threonine phosphorylation of IL-2Rbeta, but not IL-2Rgamma. To investigate the regulation of serine/threonine phosphorylation in IL-2 signaling, the roles of protein phosphatase 1 (PP1) and 2A (PP2A) were examined. Inhibition of phosphatase activity by calyculin A treatment of YT cells resulted in a significant induction of serine phosphorylation of JAK3 and STAT5, and serine/threonine phosphorylation of IL-2Rbeta. Moreover, inhibition of PP2A, but not PP1, diminished IL-2-induced tyrosine phosphorylation of IL-2Rbeta, JAK3, and STAT5, and abolished STAT5 DNA binding activity. Serine/threonine phosphorylation of IL-2Rbeta by a staurosporine-sensitive kinase also blocked its association with JAK3 and IL-2Rgamma in YT cells. Taken together, these data indicate that serine/threonine phosphorylation negatively regulates IL-2 signaling at multiple levels, including receptor complex formation and JAK3/STAT5 activation, and that this regulation is counteracted by PP2A. These findings also suggest that PP2A may serve as a therapeutic target for modulating JAK3/STAT5 activation in human disease.
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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.