has a Stoichiometric coefficient of 2 Authored: Ray, KP, 2010-05-17 Edited: Jupe, S, 2011-05-06 Reviewed: Puck, J, 2011-11-03 Multiple observations support a role for IL7-stimulated JAK/STAT signaling. IL7 induces rapid and dose-dependent tyrosine phosphorylation of JAKs 1 and 3, with concomitant tyrosine phosphorylation and DNA-binding activity of STAT5a/b (Foxwell et al. 1995). IL7RA was shown to directly induce the activation of JAKs and STATs 1, 5, and 3 by van der Plas et al. (1996). In primary human T cells and NK cells, IL7 induced activation of STAT5a, STAT5b and to a lesser extent STAT1 and STAT3 (Yu et al. 1998). Jak1 and Jak3 knockout mice displayed severely impaired thymic development, further supporting their importance in IL7 signaling (Rodig et al. 1998, Nosaka et al. 1995).<br><br> In human thymocytes, IL7 activates STAT5. It is thought that phosphorylated Y449 in the cytoplasmic domain of the IL7RA is a docking site for STAT5 (Pallard et al. 1999). STAT5 can be activated in COS 7 cells when co transfected with JAK3 (Lin et al. 1996), though this does not demonstrate that JAK3 phosphorylates STAT5 proteins in response to IL7 in vivo (Lin & Leonard, 2000); it is not clear which JAK kinase phosphorylates STAT5 in vivo. T-cells from an IL7RA Y449F knock-in mouse did not activate STAT5 (Osbourne et al. 2007), indicating that Tyr449 is a key residue regulating IL7 mediated STAT5 activation. STAT3 is critical for early B cell differentiation, but the details of its involvement are unclear (Chou et al 2006).

http://purl.obolibrary.org/obo/HINO_0006396

has a Stoichiometric coefficient of 2

Authored: Ray, KP, 2010-05-17

Edited: Jupe, S, 2011-05-06

Reviewed: Puck, J, 2011-11-03

Multiple observations support a role for IL7-stimulated JAK/STAT signaling. IL7 induces rapid and dose-dependent tyrosine phosphorylation of JAKs 1 and 3, with concomitant tyrosine phosphorylation and DNA-binding activity of STAT5a/b (Foxwell et al. 1995). IL7RA was shown to directly induce the activation of JAKs and STATs 1, 5, and 3 by van der Plas et al. (1996). In primary human T cells and NK cells, IL7 induced activation of STAT5a, STAT5b and to a lesser extent STAT1 and STAT3 (Yu et al. 1998). Jak1 and Jak3 knockout mice displayed severely impaired thymic development, further supporting their importance in IL7 signaling (Rodig et al. 1998, Nosaka et al. 1995).

In human thymocytes, IL7 activates STAT5. It is thought that phosphorylated Y449 in the cytoplasmic domain of the IL7RA is a docking site for STAT5 (Pallard et al. 1999). STAT5 can be activated in COS 7 cells when co transfected with JAK3 (Lin et al. 1996), though this does not demonstrate that JAK3 phosphorylates STAT5 proteins in response to IL7 in vivo (Lin & Leonard, 2000); it is not clear which JAK kinase phosphorylates STAT5 in vivo. T-cells from an IL7RA Y449F knock-in mouse did not activate STAT5 (Osbourne et al. 2007), indicating that Tyr449 is a key residue regulating IL7 mediated STAT5 activation. STAT3 is critical for early B cell differentiation, but the details of its involvement are unclear (Chou et al 2006).

Pubmed7481769

Pubmed10367898

Pubmed7489741

Pubmed9715265

Pubmed8709637

Pubmed8631883

Reactome, http://www.reactome.org

Pubmed17325202

Pubmed9590172

Pubmed10851055

Pubmed16825489

http://purl.obolibrary.org/obo/HINO_0009789

http://purl.obolibrary.org/obo/CHEBI_15422

http://purl.obolibrary.org/obo/HINO_0009792

http://purl.obolibrary.org/obo/CHEBI_16761

p(Y449)-IL7RA mediates STAT5 activation

HINO:0006396

p(Y449)-IL7RA mediates STAT5 activation

ReactomeREACT_115766

Reactome Database ID Release 431295540

http://purl.obolibrary.org/obo/INO_0000040