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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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N-domain-dependent nonphosphorylated STAT4 dimers required for cytokine-driven activation.

The N-terminal protein interaction domain (N-domain) of the signal transducer and activator of transcription-4 (STAT4) is believed to stabilize interactions between two phosphorylated STAT4 dimers to form STAT4 tetramers. Here, we show that nonphosphorylated STAT4 dimers form in vivo before cytokine receptor-driven activation. Mutations in the N-domain dimerization interface abolished assembly of nonphosphorylated STAT4 dimers and prevented STAT4 phosphorylation mediated by cytokine receptors. In addition, N-domain dimerization occurred for other STAT family members but was homotypic in character. This implies a conserved role for N-domain dimerization, which might include influencing interactions with cytokine receptors, favoring homodimer formation or accelerating formation of the phosphorylated STAT dimer.[1]

References

  1. N-domain-dependent nonphosphorylated STAT4 dimers required for cytokine-driven activation. Ota, N., Brett, T.J., Murphy, T.L., Fremont, D.H., Murphy, K.M. Nat. Immunol. (2004) [Pubmed]
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