STAT1 signaling is not regulated by a phosphorylation-acetylation switch.

A phosphorylation-acetylation switch regulates STAT1 signaling.

Cytokines such as interferons (IFNs) activate signal transducers and activators of transcription (STATs) via phosphorylation. Histone deacetylases (HDACs) and the histone acetyltransferase (HAT) CBP dynamically regulate STAT1 acetylation. Here we show that acetylation of STAT1 counteracts IFN-induced STAT1 phosphorylation, nuclear translocation, DNA binding, and target gene expression. Biochemi...

Antunes , Filipa and Marg , Andreas and Vinkemeier , Uwe ( 2011 ) STAT 1 signaling is not regulated by a phosphorylation - acetylation switch

Acetylation at Lys-92 enhances signaling by the chemotaxis response regulator protein CheY.

When Escherichia coli cells lacking all chemotaxis proteins except the response regulator CheY are exposed to acetate, clockwise flagellar rotation results, indicating the acetate stimulus has activated signaling by CheY. Acetate can be converted to acetyl-CoA by either of two different metabolic pathways, which proceed through acetyl phosphate or acetyl-AMP intermediates. In turn, CheY can be ...

Post-translational modifications of proteins in gene regulation under hypoxic conditions

Hypoxia is a common feature of highly proliferating tissues and tissues with inflammation. The transcriptional response to hypoxia involves activation of signal transduction pathways, which is mainly mediated by post-translational modifications of signaling molecules, transcription factors and histones. Activation of hypoxia responsive transcription factors HIF and NF-κB is a subject of regulat...

An acetylation–phosphorylation switch that regulates tau aggregation propensity and function

The aberrant accumulation of tau protein is a pathological hallmark of a class of neurodegenerative diseases known as tauopathies, including Alzheimer's disease and related dementias. On the basis of previous observations that tau is a direct substrate of histone deacetylase 6 (HDAC6), we sought to map all HDAC6-responsive sites in tau and determine how acetylation in a site-specific manner aff...