Phosphorylated Stat3 Forms Dimer

Stable Identifier
R-MMU-2730597
Type
Reaction [binding]
Species
Mus musculus
Compartment
General
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Phosphorylated Stat3 Forms Dimer

Both unphosphorylated and phosphorylated Stat3 can form dimers, however the dimers formed by phosphorylated Stat3 have a different conformation and activate transcription more effectively.

Literature References
PubMed ID Title Journal Year
10642496 Cytoplasmic STAT proteins associate prior to activation

Haan, S, Kortylewski, M, Behrmann, I, Müller-Esterl, W, Schaper, F

Biochem. J. 2000
8140422 Stat3: a STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6

Zhong, Z, Wen, Z, Darnell JE, Jr

Science 1994
21325026 The role of the N-terminal domain in dimerization and nucleocytoplasmic shuttling of latent STAT3

Vogt, M, Domoszlai, T, Kleshchanok, D, Lehmann, S, Schmitt, A, Poli, V, Richtering, W, Müller-Newen, G

J. Cell. Sci. 2011
Participants
Orthologous Events
Authored
Reviewed
Created