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Details on Person Activated JAK2 binds to unphosphorylated STAT5; cytokine tre...
| Class:Id | Summation:879950 |
|---|---|
| _displayName | Activated JAK2 binds to unphosphorylated STAT5; cytokine tre... |
| _timestamp | 2010-10-05 12:46:59 |
| created | [InstanceEdit:879892] Jupe, S, 2010-06-25 |
| literatureReference | [LiteratureReference:975840] Interleukin-3, granulocyte-macrophage colony stimulating factor and interleukin-5 transduce signals through two STAT5 homologs [LiteratureReference:975847] Interleukin-3, granulocyte-macrophage colony-stimulating factor, and interleukin-5 transduce signals through two forms of STAT5 [LiteratureReference:914207] Pathways in cytokine regulation of hematopoiesis [LiteratureReference:914079] Cell growth arrest and induction of cyclin-dependent kinase inhibitor p21 WAF1/CIP1 mediated by STAT1 [LiteratureReference:893556] IL-3 signaling and the role of Src kinases, JAKs and STATs: a covert liaison unveiled [LiteratureReference:914210] STATs and gene regulation [LiteratureReference:507804] Stat5a and Stat5b proteins have essential and nonessential, or redundant, roles in cytokine responses [LiteratureReference:507782] Stat recruitment by tyrosine-phosphorylated cytokine receptors: an ordered reversible affinity-driven process [LiteratureReference:904798] Functional subdomains of STAT2 required for preassociation with the alpha interferon receptor and for signaling [LiteratureReference:975842] IL-5 and granulocyte-macrophage colony-stimulating factor activate STAT3 and STAT5 and promote Pim-1 and cyclin D3 protein expression in human eosinophils [LiteratureReference:975837] Activation of the STAT3/acute phase response factor transcription factor by interleukin-5 [LiteratureReference:975844] In vitro analysis of STAT5 activation by granulocyte-macrophage colony-stimulating factor [LiteratureReference:879924] Mechanism of activation of the GM-CSF, IL-3, and IL-5 family of receptors [LiteratureReference:904797] In vitro interaction between STAT 5 and JAK 2; dependence upon phosphorylation status of STAT 5 and JAK 2 [LiteratureReference:904800] Signaling functions of the tyrosine residues in the betac chain of the granulocyte-macrophage colony-stimulating factor receptor [LiteratureReference:914201] Cytoplasmic domains of the common beta-chain of the GM-CSF/IL-3/IL-5 receptors that are required for inducing differentiation or clonal suppression in myeloid leukaemic cell lines |
| modified | [InstanceEdit:904809] Jupe, S, 2010-07-02 [InstanceEdit:909735] Jupe, S, 2010-07-07 [InstanceEdit:914066] Jupe, S, 2010-07-21 [InstanceEdit:914176] Jupe, S, 2010-07-23 [InstanceEdit:914195] Jupe, S, 2010-07-23 [InstanceEdit:941868] Jupe, S, 2010-09-06 [InstanceEdit:975839] Jupe, S, 2010-10-05 |
| text | Activated JAK2 binds to unphosphorylated STAT5; cytokine treatment of cells leads to JAK2 activation and promotes binding of JAK2 to unphosphorylated STAT5. STAT5 proteins are considered the main targets of IL-3, IL-5 and GM-CSF signaling (Mui et al. 1995a, Mui et al. 1995b, Ihle, 2001), but other members of this family including STAT3 and STAT1 (Chin et al. 1996) can be involved, the STAT family member activated appears to depend on the cell line used in the study, rather than the cytokine (Reddy et al. 2000). IL-5 and GM-CSF increase STAT3 and 5 signaling (Caldenhoven et al. 1995, Stout et al. 2004). Unphosphorylated STATs are cytoplasmic; tyrosine phosphorylation facilitates dimerization and translocation to the nucleus where they act as transcription factors. STATs were originally described as ligand-induced transcription factors in interferon-treated cells, subsequently they were shown to be critical in many signal transduction pathways associated with cytokines and neurokines including several interleukins, the interferons, erythropoietin, prolactin, growth hormone, oncostatin M (OSM), and ciliary neurotrophic factor (Darnell 1997, Reddy et al. 2000). JAK-STAT signaling is widely accepted as a primary signaling route for receptors that share the common beta subunit (Bc). The role of the receptor itself in STAT5 binding is somewhat controversial because while STAT proteins can be recruited to tyrosine phosphorylated receptors via their SH2 domains (Greenlund et al. 1995, Li et al. 1997) binding of STAT5 to Bc has not been formally demonstrated (Guthridge et al. 1998), though tyrosine-phosphorylated peptides of Bc have been demonstrated to associate with STAT5, and anti-Bc or phosphotyrosine antibodies inhibited GM-CSF induced STAT5 DNA binding activity (Sakurai et al. 2000). Binding of JAK2 to STAT5 can occur in vitro when no receptor is present (Flores-Morales et al. 1998). STAT5 activation was seen when all six conserved cytoplasmic tyrosines in Bc were mutated to P (Okuda et al. 1997), but a C-terminal deletion mutant of Bc while able to activate JAK2 was unable to activate STAT5 (Smith et al. 1997). These observations suggest that JAK2 activation is a critical step in STAT signaling from Bc-containing receptors, but other factors may be required. It is not clear whether Bc is directly involved or not in STAT5 activation, but the specificity for particular STAT members is believed to be determined by STAT docking sites present on the receptor molecules, not JAK kinase preference (Reddy et al. 2000). |
| (summation) | [Reaction:879930] STAT5 is recruited by JAK2 [Homo sapiens] |
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