Reactome | p-Y-STATs dimerize

p-Y-STATs dimerize

Stable Identifier

R-HSA-6788622

Type

Reaction [omitted]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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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
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
12832402	STATs dimerize in the absence of phosphorylation Olson, R, Schindler, C, Braunstein, J, Brutsaert, S	J. Biol. Chem.	2003