| First Author | Ota N | Year | 2004 |
| Journal | Nat Immunol | Volume | 5 |
| Issue | 2 | Pages | 208-15 |
| PubMed ID | 14704793 | Mgi Jnum | J:331653 |
| Mgi Id | MGI:7388705 | Doi | 10.1038/ni1032 |
| Citation | Ota N, et al. (2004) N-domain-dependent nonphosphorylated STAT4 dimers required for cytokine-driven activation. Nat Immunol 5(2):208-15 |
| abstractText | 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. |
