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Cell Signal. 2013 Sep;25(9):1924-31. doi: 10.1016/j.cellsig.2013.05.007. Epub 2013 May 22.

Regulation of STAT signaling by acetylation.

Author information

1
Department of Nephrology, Shanghai East Hospital, Tongji University School of Medicine, Shanghai 200120, China. szhuang@lifespan.org

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.

PMID:
23707527
PMCID:
PMC4550442
DOI:
10.1016/j.cellsig.2013.05.007
[Indexed for MEDLINE]
Free PMC Article

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