Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
Volume 1862, Issue 10, Pages 1871-1882Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbadis.2016.07.005
Keywords
Protein phosphorylation; Alzheimer disease; p53; Insulin; Proteomics
Funding
- Fondi di Ateneo Sapienza
- People Programme (Marie Curie Actions) of the European Union's Seventh Framework Programme (FP7) under REA grant [624341]
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Protein phosphorylation of serine, threonine, and tyrosine residues is one of the most prevalent post translational modifications fundamental in mediating diverse cellular functions in living cells. Aberrant protein phosphorylation is currently recognized as a critical step in the pathogenesis and progression of Alzheimer disease (AD). Changes in the pattern of protein phosphorylation of different brain regions are suggested to promote AD transition from a presymptomatic to a symptomatic state in response to accumulating amyloid peptide (A beta). Several experimental approaches have been utilized to profile alteration of protein phosphorylation in the brain, including proteomics. Among central pathways regulated by kinases/phosphatases those involved in the activation/inhibition of both pro survival and cell death pathways play a central role in AD pathology. We discuss in detail how aberrant phosphorylation could contribute to dysregulate p53 activity and insulin mediated signaling. Taken together these results highlight that targeted therapeutic intervention, which can restore phosphorylation homeostasis, either acting on kinases and phosphatases, conceivably may prove to be beneficial to prevent or slow the development and progression of AD. (C) 2016 Elsevier B.V. All rights reserved.
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