Journal
EXPERIMENTAL NEUROLOGY
Volume 271, Issue -, Pages 77-83Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.expneurol.2015.05.003
Keywords
Neurodegenerative diseases; Protein kinase B (Akt); Protein arginine methyltransferase (PRMT); Serine phosphorylation; Arginine methylation
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Funding
- Telethon-Italy [TCP12013]
- Italian Ministry of Heath [RF-2011-02350097]
- Associazione Alzheimer Trento Onlus
- CIBIO internal funds
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Neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, polyglutamine diseases and motor neuron diseases, are late-onset and progressive disorders characterized by the accumulation of misfolded proteins inside and outside neurons. No effective therapies exist to delay the onset or arrest the progression of these diseases. One novel and promising therapeutic approach consists of targeting disease-causing proteins at the post-translational level. Here we illustrate this concept using the example of spinal and bulbar muscular atrophy, a neurodegenerative disease caused by polyglutamine expansion in the androgen receptor. Emerging evidence suggests that two key post-translational modifications of polyglutamine-expanded androgen receptor, namely serine phosphotylation by protein kinase B/Akt and arginine methylation by protein arginine methyl-transferases, occur at the same consensus site, are mutually exclusive, and have opposing effects on neurotoxicity. Because several proteins linked to neurodegenerative diseases have canonical Akt consensus site motifs, these findings may have a broad impact in the field of neurological diseases caused by misfolded proteins. (C) 2015 Elsevier Inc. All rights reserved.
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