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STAT1 signaling is not regulated by a phosphorylation-acetylation switch

Antunes, Filipa; Marg, Andreas; Vinkemeier, Uwe

Authors

Filipa Antunes

Andreas Marg

Uwe Vinkemeier



Abstract

The treatment of cells with histone deacetylase inhibitors (HDACi) was reported to reveal the acetylation of
STAT1 at lysine 410 and lysine 413 (O. H. Kra¨mer et al., Genes Dev. 20:473–485, 2006). STAT1 acetylation was
proposed to regulate apoptosis by facilitating binding to NF-B and to control immune responses by suppressing
STAT1 tyrosine phosphorylation, suggesting that STAT1 acetylation is a central mechanism by which
histone deacetylase inhibitors ameliorate inflammatory diseases (O. H. Kra¨mer et al., Genes Dev. 23:223–235,
2009). Here, we show that the inhibition of deacetylases had no bearing on STAT1 acetylation and did not
diminish STAT1 tyrosine phosphorylation. The glutamine mutation of the alleged acetylation sites, claimed to
mimic acetylated STAT1, similarly did not diminish the tyrosine phosphorylation of STAT1 but precluded its
DNA binding and nuclear import. The defective transcription activity of this mutant therefore cannot be
attributed to STAT1 acetylation but rather to the inactivation of the STAT1 DNA binding domain and its
nuclear import signal. Experiments with respective cDNAs provided by the authors of the studies mentioned
above confirmed the results reported here, further questioning the validity of the previous data. We conclude
that the effects and potential clinical benefits associated with histone deacetylase inhibition cannot be explained by promoting the acetylation of STAT1 at lysines 410 and 413.

Journal Article Type Article
Publication Date Jul 1, 2011
Journal Molecular and Cellular Biology
Print ISSN 0270-7306
Electronic ISSN 0270-7306
Publisher American Society for Microbiology
Peer Reviewed Peer Reviewed
Volume 31
Issue 14
APA6 Citation Antunes, F., Marg, A., & Vinkemeier, U. (2011). STAT1 signaling is not regulated by a phosphorylation-acetylation switch. Molecular and Cellular Biology, 31(14), doi:10.1128/MCB.05300-11
DOI https://doi.org/10.1128/MCB.05300-11
Publisher URL http://mcb.asm.org/content/31/14/3029.
Copyright Statement Copyright information regarding this work can be found at the following address: http://eprints.nottingh.../end_user_agreement.pdf

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Copyright Statement
Copyright information regarding this work can be found at the following address: http://eprints.nottingham.ac.uk/end_user_agreement.pdf





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