| Literature DB >> 26227998 |
Wagner Carbolin Martins1, Carla Inês Tasca1, Helena Cimarosti2.
Abstract
SUMO (small ubiquitin-like modifier) conjugation is a critically important control process in all eukaryotic cells, because it acts as a biochemical switch and regulates the function of hundreds of proteins in many different pathways. Although the diverse functional consequences and molecular targets of SUMOylation remain largely unknown, SUMOylation is becoming increasingly implicated in the pathophysiology of Alzheimer's disease (AD). Apart from the central SUMO-modified disease-associated proteins, such as amyloid precursor protein, amyloid β, and tau, SUMOylation also regulates several other processes underlying AD. These are involved in inflammation, mitochondrial dynamics, synaptic transmission and plasticity, as well as in protective responses to cell stress. Herein, we review current reports on the involvement of SUMOylation in AD, and present an overview of potential SUMO targets and pathways underlying AD pathogenesis.Entities:
Keywords: Alzheimer’s disease; Inflammation; Neuroprotection; SUMO; Synaptic plasticity
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Year: 2015 PMID: 26227998 DOI: 10.1007/s11064-015-1681-3
Source DB: PubMed Journal: Neurochem Res ISSN: 0364-3190 Impact factor: 3.996