Phosphorylated Stat5 dimerizes

Stable Identifier
R-MMU-2730593
Type
Reaction [binding]
Species
Mus musculus
Compartment
ReviewStatus
5/5
General
SVG |   | PPTX  | SBGN
Phosphorylated Stat5 dimerizes
After phosphorylation, Stat5a and Stat5b form homodimers and heterodimers in the cytosol (Cella et al. 1998, Boehm et al. 2014). 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 (Fahrenkamp et al. 2016)
Literature References
PubMed ID Title Journal Year
27752093 Intramolecular hydrophobic interactions are critical mediators of STAT5 dimerization

Chatain, N, Fahrenkamp, D, Küster, A, Müller-Newen, G, Li, J, Schmitz-Van De Leur, H, Rossetti, G, Lüscher, B, Koschmieder, S, Ernst, S

Sci Rep 2016
25333863 Identification of isoform-specific dynamics in phosphorylation-dependent STAT5 dimerization by quantitative mass spectrometry and mathematical modeling

Boehm, ME, Schilling, M, Adlung, L, Lehmann, WD, Klingmüller, U, Roth, S

J. Proteome Res. 2014
9528750 Characterization of Stat5a and Stat5b homodimers and heterodimers and their association with the glucocortiocoid receptor in mammary cells

Hynes, NE, Cella, N, Groner, B

Mol Cell Biol 1998
Participants
Orthologous Events
Authored
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