p-STAT5 dimerizes

Stable Identifier
R-HSA-452102
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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Phosphorylated STAT5A and STAT5B form homodimers and heterodimers in the cytosol (Gaffen et al. 1996, Rosenthal et al. 1997, also inferred from mouse homologs). Phosphorylation of a critical tyrosine residue in the SH domain (Y694 in STAT5A and Y699 in STAT5B) and intramolecular interactions between hydrophobic residues in the SH domain are required for dimerization (inferred from mouse homologs).

Literature References
PubMed ID Title Journal Year
8702919 Distinct tyrosine residues within the interleukin-2 receptor beta chain drive signal transduction specificity, redundancy, and diversity

Gaffen, SL, Lai, SY, Ha, M, Liu, X, Hennighausen, L, Greene, WC, Goldsmith, MA

J Biol Chem 1996
9398404 IL-2 and IL-7 induce heterodimerization of STAT5 isoforms in human peripheral blood T lymphoblasts

Rosenthal, LA, Winestock, KD, Finbloom, DS

Cell Immunol 1997
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