p-Y705-STAT3 dimer translocates from cytosol to nucleoplasm

Stable Identifier
Reaction [uncertain]
Homo sapiens
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The classical model of JAK-STAT signaling suggests that phosphorylated Signal transducer and activator of transcription 3 (STAT3) translocates to the nucleus (Akira et al. 1994) where it binds DNA to mediate the effects of Interleukin-10 (IL10) on expression of cytokines, soluble mediators and cell surface molecules by cells of myeloid origin, with important consequences for their ability to activate and sustain immune and inflammatory responses. STAT3 is able to shuttle freely between the cytoplasm and the nucleus, independent of tyrosine phosphorylation (Liu et al. 2005, Li 2008, Reich 2013). Binding of unphosphorylated STAT3 to DNA has been reported (Nkansah et al. 2013). As it is not clear what triggers nuclear accumulation of STAT3 in response to IL10 this event is shown as an uncertain process.
Literature References
PubMed ID Title Journal Year
15919823 STAT3 nuclear import is independent of tyrosine phosphorylation and mediated by importin-alpha3

Reich, NC, McBride, KM, Liu, L

Proc. Natl. Acad. Sci. U.S.A. 2005
7512451 Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-related transcription factor involved in the gp130-mediated signaling pathway

Kishimoto, T, Naruto, M, Wang, XJ, Yoshida, K, Nishio, Y, Wei, S, Sudo, T, Akira, S, Matsusaka, T, Inoue, M

Cell 1994
12554859 New microRNAs from mouse and human

Lagos-Quintana, M, Tuschl, T, Borkhardt, A, Meyer, J, Rauhut, R

RNA 2003
Orthologous Events
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