ArticleThe EMBO journal2006
Receptor specific downregulation of cytokine signaling by autophosphorylation in the FERM domain of Jak2.
Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 73 citations in OpenAlex.
- JAK2 46/1 (GGCC) Haplotype in Oncogenesis, as Risk Stratifier, and Indicator for Drug Resistance in Myeloproliferative Neoplasms.International journal of molecular sciences · 2025Review
- JAK/STAT in human diseases: a common axis in immunodeficiencies and hematological disorders.Frontiers in immunology · 2025Review
- Growth Hormone Receptor Regulation in Cancer and Chronic Diseases.Frontiers in endocrinology · 2020Review
- Activating JAK2 mutants reveal cytokine receptor coupling differences that impact outcomes in myeloproliferative neoplasm.Leukemia · 2017Article
- A mouse model reveals that Mfsd2a is critical for unfolded protein response upon exposure to tunicamycin.Human cell · 2017Article
- Three Tyrosine Residues in the Erythropoietin Receptor Are Essential for Janus Kinase 2 V617F Mutant-induced Tumorigenesis.The Journal of biological chemistry · 2017Article
- Fos-Zippered GH Receptor Cytosolic Tails Act as Jak2 Substrates and Signal Transducers.Molecular endocrinology (Baltimore, Md.) · 2016Article
- Crystal Structure of the FERM-SH2 Module of Human Jak2.PloS one · 2016Article
- The molecular regulation of Janus kinase (JAK) activation.The Biochemical journal · 2014Review
- Drosophila SOCS36E negatively regulates JAK/STAT pathway signaling via two separable mechanisms.Molecular biology of the cell · 2013Article
- Janus kinase 3: the controller and the controlled.Acta biochimica et biophysica Sinica · 2012Review
- Phosphorylation of Y372 is critical for Jak2 tyrosine kinase activation.Cellular signalling · 2011Article
- FERM domain mutations induce gain of function in JAK3 in adult T-cell leukemia/lymphoma.Blood · 2011Article
- Analysis of Jak2 catalytic function by peptide microarrays: the role of the JH2 domain and V617F mutation.PloS one · 2011Article
- Jak2 is a negative regulator of ubiquitin-dependent endocytosis of the growth hormone receptor.PloS one · 2011Article
- A structure-function perspective of Jak2 mutations and implications for alternate drug design strategies: the road not taken.Current medicinal chemistry · 2011Review
- Jak/STAT pathways in cytokine signaling and myeloproliferative disorders: approaches for targeted therapies.Genes & cancer · 2010Article
- Megakaryopoiesis.Seminars in hematology · 2010Review
- Tyrosines 868, 966, and 972 in the kinase domain of JAK2 are autophosphorylated and required for maximal JAK2 kinase activity.Molecular endocrinology (Baltimore, Md.) · 2010Article
- STAT5 activation is critical for the transformation mediated by myeloproliferative disorder-associated JAK2 V617F mutant.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The tyrosine kinase, Janus kinase-2 (Jak2), plays a pivotal role in signal transduction through a variety of cytokine receptors, including the receptor for erythropoietin (Epo). Although the physiological relevance of Jak2 has been definitively established, less is known about its regulation. In studies assessing the roles of sites of tyrosine phosphorylation, we identified Y(119) in the FERM (band 4.1, Ezrin, radixin and moesin) domain as a phosphorylation site. In these studies, we demonstrate that the phosphorylation of Y(119) in response to Epo downregulates Jak2 kinase activity. Using a phosphorylation mimic mutation (Y(119)E), downregulation is shown to involve dissociation of Jak2 from the receptor complex. Conversely, a Y(119)F mutant is more stably associated with the receptor complex. Thus, in cytokine responses, ligand binding induces activation of receptor associated Jak2, autophosphorylation of Y(119) in the FERM domain and the subsequent dissociation of the activated Jak2 from the receptor and degradation. This regulation occurs with the receptors for Epo, thrombopoietin and growth hormone but not with the receptor for interferon-gamma.
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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.