Activation of Stat3 sequence-specific DNA binding and transcription by p300/CREB-binding protein-mediated acetylation
UMass Chan Affiliations
Department of Cancer BiologyDocument Type
Journal ArticlePublication Date
2005-01-15Keywords
AcetylationActive Transport, Cell Nucleus
Cells, Cultured
DNA
DNA-Binding Proteins
Humans
Nuclear Proteins
STAT3 Transcription Factor
Trans-Activators
*Transcription, Genetic
Life Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
Signal transducers and activators of transcription (Stat) belong to a family of latent cytoplasmic factors that can be activated by tyrosine phosphorylation by 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. Here we report for the first time that Stat3 can be modified by acetylation both in vivo and in vitro. A major site of Stat3 that is acetylated by its coactivator, p300/CREB-binding protein (CBP), resides in the C-terminal transcriptional activation domain at lysine 685. Furthermore, the acetylation of Stat3 can stimulate its sequence-specific DNA binding ability and transactivation activity. Inhibition of histone deacetylase activity in cells results in increased Stat3 nuclear localization. These observations clearly indicate a novel mechanism for Stat3 activation in mammalian cells.Source
J Biol Chem. 2005 Mar 25;280(12):11528-34. Epub 2005 Jan 13. Link to article on publisher's siteDOI
10.1074/jbc.M413930200Permanent Link to this Item
http://hdl.handle.net/20.500.14038/42337PubMed ID
15649887Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1074/jbc.M413930200