p-Y705-STAT3 dimerizes

Stable Identifier
Reaction [uncertain]
Homo sapiens
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Phosphorylated Signal transducer and activator of transcription 3 (STAT3) dimerizes after dissociating from the interleukin-19 (IL19) receptor complex (Akira et al. 1994) or Interleukin-22 (IL22) receptor complex (Lagos-Quintana et al. 2003, Sestito et al. 2011).

According to the classical model, phosphorylated Signal transducer and activator of transcription (STAT) monomers associate in an active dimer form, which is stabilized by the reciprocal interactions between a phosphorylated tyrosine residue of one and the SH2 domain of the other monomer (Shuai et al. 1994). These dimers then translocate to the nucleus (Akira et al. 1994). Recently an increasing number of studies have demonstrated the existence of STAT dimers in unstimulated cell states and the capability of STATs to exert biological functions independently of phosphorylation (Braunstein et al. 2003, Li et al. 2008, Santos & Costas-Pereira 2011). As phosphorylation of STATs is not unequivocally required for its subsequent translocation to the nucleus, this event is shown as an uncertain process.

Literature References
PubMed ID Title Journal Year
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
7510216 Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions

Cowburn, D, Horvath, CM, Huang, LH, Darnell JE, Jr, Qureshi, SA, Shuai, K

Cell 1994
12554859 New microRNAs from mouse and human

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

RNA 2003
12832402 STATs dimerize in the absence of phosphorylation

Olson, R, Schindler, C, Braunstein, J, Brutsaert, S

J. Biol. Chem. 2003
Orthologous Events
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