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Post-translational modifications in neurodegeneration

1 Department of Neurology, University of California San Francisco, San Francisco, CA 94158, USA
2 ECSIN-European Center for the Sustainable Impact of Nanotechnology, Viale Porta Adige 45, I-45100 Rovigo, Italy

Topical Section: Post-translational modification

Post-translational modifications increase proteome functionality for managing all aspects of normal cell biology. They are based on the covalent attachment of functional groups, leading to phosphorylation, acetylation, glycosylation, acylation, ubiquitination, SUMOylation and oxidation of protein targets. Post-translational modifications occur at any step of protein life cycle, modulating in time and space protein folding, subcellular localization and activity. Aberrant post-translational modifications of one or more culprit proteins may lead to neurodegeneration, as shown in paradigmatic neurological disorders such as Alzheimer’s, Parkinson’s and prion diseases. In this review, we report the most important post-translational modifications found in neurodegenerative disorders, illustrating the pathophysiological mechanisms in which they are involved. This work highlights the lack of a global framework of post-translational modifications in terms of complexity and regulation. Therefore, in the next future many efforts are required to describe the interplay existing between post-translational modifications and their combinatorial patterns on protein targets.
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Keywords post-translational modifications; neurodegeneration; phosphorylation; acetylation; glycosylation; acylation; ubiquitination; SUMOylation; deamidation; oxidation

Citation: Alessandro Didonna, Federico Benetti. Post-translational modifications in neurodegeneration. AIMS Biophysics, 2016, 3(1): 27-49. doi: 10.3934/biophy.2016.1.27

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