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Review
, 25 (9), 1924-31

Regulation of STAT Signaling by Acetylation

Affiliations
Review

Regulation of STAT Signaling by Acetylation

Shougang Zhuang. Cell Signal.

Abstract

Signal transducers and activators of transcription (STAT) belong to a family of latent cytoplasmic factors that can be activated by tyrosine phosphorylation by the members of the Jak tyrosine kinase family in response to a variety of cytokines and growth factors. Activated STATs form dimers and translocate into nucleus to induce expression of critical genes essential for normal cellular events. In the past several years, significant progress has been made in the characterization of STAT acetylation, which is dependent on the balance between histone deacetylases (HDACs) and histone acetyltransferases (HATs) such as CBP/p300. Acetylation of STAT1, STAT2, STAT3, STAT5b and STAT6 has been identified. This review will highlight acetylation on the modulation of STAT activation.

Figures

Figure 1
Figure 1
Structure of STAT proteins with the most important conserved domains. P is phosphorylation sites.
Figure 2
Figure 2
Regulation of STAT3 dimerization by acetylation. CBP/p300 induces STAT3 acetylation, which is required for its dimerization and subsequent nuclear translocation and gene transcription. On the contrary, HDACs promote STAT3 deacetylation.
Figure 3
Figure 3
Acetylation of IFNαR-ISGF3 pathway is required for the antiviral activity of IFNα. Upon stimulation with IFNα, CBP is translocated from the nucleus to the cytosol and induces IFNαR acetylation on Lys 399. IRF9 interacts with this acetylation site leads to formation of the ISGF3 complex, which includes IRF9, STAT1 and STAT2. This complex is then translocated to the nucleus where it binds DNA and drives gene expression.

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