ArticleOncogene2011
Phosphorylation of p27Kip1 by JAK2 directly links cytokine receptor signaling to cell cycle control.
Article in Oncogene, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 64 citations in OpenAlex.
- G0 or no-G0: phosphatase control of quiescence and cell cycle entry.Biochemical Society transactions · 2026Review
- The deacetylases HDAC1/HDAC2 control JAK2Signal transduction and targeted therapy · 2025Article
- CDKN1B (p27/kip1) enhances drug-tolerant persister CTCs by restricting polyploidy following mitotic inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Artificial neural network inference analysis identified novel genes and gene interactions associated with skeletal muscle aging.Journal of cachexia, sarcopenia and muscle · 2024Article
- Essential contribution of the JAK/STAT pathway to carcinogenesis, lytic infection of herpesviruses and pathogenesis of COVID‑19 (Review).Molecular medicine reports · 2024Review
- Article
- ACK1 upregulated the proliferation of head and neck squamous cell carcinoma cells by promoting p27 phosphorylation and degradation.Journal of cell communication and signaling · 2022Article
- JAK2-CHK2 signaling safeguards the integrity of the mitotic spindle assembly checkpoint and genome stability.Cell death & disease · 2022Article
- Chromosome Genome Assembly ofGenes · 2021Article
- Stimulation of c-Jun/AP-1-Activity by the Cell Cycle Inhibitor p57Frontiers in cell and developmental biology · 2021Article
- The CDK inhibitor p57Scientific reports · 2020Article
- MIAT inhibits proliferation of cervical cancer cells through regulating miR-150-5p.Cancer cell international · 2020Article
- JAK2 Inhibition Impairs Proliferation and Sensitises Cervical Cancer Cells to Cisplatin-Induced Cell Death.Cancers · 2019Article
- Network Pharmacology Identifies the Mechanisms of Action of Shaoyao Gancao Decoction in the Treatment of Osteoarthritis.Medical science monitor : international medical journal of experimental and clinical research · 2019Article
- Clonal Hematopoiesis: Somatic Mutations in Blood Cells and Atherosclerosis.Circulation. Genomic and precision medicine · 2018Review
- A single nucleotide polymorphism of cyclin-dependent kinase inhibitor 1B (p27Journal of vascular surgery · 2018Article
- FLT3 and FLT3-ITD phosphorylate and inactivate the cyclin-dependent kinase inhibitor p27Haematologica · 2017Article
- Review
- Phosphoserine aminotransferase 1 is associated to poor outcome on tamoxifen therapy in recurrent breast cancer.Scientific reports · 2017Article
- Suppressor of Cytokine Signaling 2 Negatively Regulates NK Cell Differentiation by Inhibiting JAK2 Activity.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Janus kinase 2 (JAK2) couples ligand activation of cell surface cytokine receptors to the regulation of cellular functions including cell cycle progression, differentiation and apoptosis. It thereby coordinates biological programs such as development and hematopoiesis. Unscheduled activation of JAK2 by point mutations or chromosomal translocations can induce hyperproliferation and hematological malignancies. Typical signal transduction by the JAK2 tyrosine kinase comprises phosphorylation of STAT transcription factors. In this study, we describe the identification of the cyclin-dependent kinase (CDK) inhibitor p27(Kip1) as a novel JAK2 substrate. JAK2 can directly bind and phosphorylate p27(Kip1). Both, the JAK2 FERM domain and its kinase domain bind to p27(Kip1). JAK2 phosphorylates tyrosine residue 88 (Y88) of p27(Kip1). We previously reported that Y88 phosphorylation of p27(Kip1) by oncogenic tyrosine kinases impairs p27(Kip1)-mediated CDK inhibition, and initiates its ubiquitin-dependent proteasomal degradation. Consistently, we now find that active oncogenic JAK2V617F reduces p27(Kip1) stability and protein levels in patient-derived cell lines harboring the mutant JAK2V617F allele. Moreover, tyrosine phosphorylation of p27(Kip1) is impaired and p27(Kip1) expression is restored upon JAK2V617F inactivation by small hairpin RNA-mediated knockdown or by the pyridone-containing tetracycle JAK inhibitor-I, indicating that direct phosphorylation of p27(Kip1) can contribute to hyperproliferation of JAK2V617F-transformed cells. Activation of endogenous JAK2 by interleukin-3 (IL-3) induces Y88 phosphorylation of p27(Kip1), thus unveiling a novel link between cytokine signaling and cell cycle control in non-transformed cells. Oncogenic tyrosine kinases could use this novel pathway to promote hyperproliferation in tumor cells.
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