Transcription factor activity of STAT proteins: structural requirements and regulation by phosphorylation and interacting proteins

Cell Mol Life Sci. 1999 Sep;55(12):1535-46. doi: 10.1007/s000180050393.


The seven mammalian members of the signal transducer and activator of transcription (STAT) family share a common core structure which reflects their shared mechanism of activation, dimerization, and DNA binding. By contrast, the STAT C termini containing the sequences required for transcriptional activation are much less homologous, suggesting different ways by which individual STATs activate their target genes. This paper describes several important discoveries linked to mechanistic aspects of STAT transcription factor function. These include regulated serine phosphorylation of the transactivating domain, promoter-dependent interactions of STATs with each other, or of STATs with other transcription factors, and with transcriptional co-activators. The basis, background, and implications of these molecular events will be summarized and discussed.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / physiology*
  • Humans
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Binding
  • Sequence Alignment
  • Signal Transduction*
  • Structure-Activity Relationship
  • Trans-Activators / chemistry
  • Trans-Activators / physiology*
  • Transcription Factors / physiology


  • DNA-Binding Proteins
  • Trans-Activators
  • Transcription Factors