Title : The two interfaces of the STAT1 N-terminus exhibit opposite functions in IFN╬│-regulated gene expression.

Pub. Date : 2015 Oct

PMID : 26275341






2 Functional Relationships(s)
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1 Our data show that four negatively charged, surface-exposed amino acid residues in the N-terminal domain dimer are engaged in the disassembly of tyrosine-phosphorylated tetrameric complexes on DNA and prevent the occurrence of higher-order STAT1 oligomers on low-affinity DNA binding sites. Tyrosine signal transducer and activator of transcription 1 Homo sapiens
2 Similarly to a STAT1 mutant with impaired tetramerization, the N-terminal gain-of-function mutants showed elevated tyrosine-phosphorylation levels and prolonged nuclear accumulation upon stimulation of cells with IFNgamma. Tyrosine signal transducer and activator of transcription 1 Homo sapiens