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Issue 11, 2006
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Structure, function, and regulation of STAT proteins

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The Signal Transducer and Activator of Transcription (STAT) family of proteins was first discovered in the 1990's as key proteins in cytokine signaling. Since then, the field has greatly advanced in the past 15 years, providing significant insight into the structure, function, and regulation of STATs. STATs are latent cytoplasmic transcription factors consisting of seven mammalian members. They are Tyr phosphorylated upon activation, a post-translational modification critical for dimerization, nuclear import, DNA binding, and transcriptional activation. In recent years, unphosphorylated STATs have also been observed to dimerize and drive transcription, albeit by yet an obscure mechanism. In addition, the function of cytoplasmic STATs is beginning to emerge. Here, we describe the structure, function, and regulation of both unphosphorylated and phosphorylated STATs. STAT isoforms from alternative splicing or proteolytic processing, and post-translational modifications affecting STAT activities are also discussed.

Graphical abstract: Structure, function, and regulation of STAT proteins

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Publication details

The article was received on 04 May 2006, accepted on 30 Aug 2006 and first published on 26 Sep 2006

Article type: Review Article
DOI: 10.1039/B606246F
Citation: Mol. BioSyst., 2006,2, 536-550

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    Structure, function, and regulation of STAT proteins

    C. P. Lim and X. Cao, Mol. BioSyst., 2006, 2, 536
    DOI: 10.1039/B606246F

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