Neddylation dysfunction in Alzheimer's disease
Name
Chen-2012-Neddylation dysfunct.pdf
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380.9 KB
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Author(s)
Chen, Yuzhi
Neve, Rachael L.
Liu, Helena
Date Issued
November 2012
Journal
Journal of Cellular and Molecular Medicine
Publisher
John Wiley & Sons, Inc
Citation
Chen, Yuzhi, Rachael L. Neve, and Helena Liu. “Neddylation Dysfunction in Alzheimer’s Disease.” J. Cell. Mol. Med. 16, no. 11 (October 29, 2012): 2583–2591.
Version
Final published version
Abstract
Ubiquitin-dependent proteolysis is a major mechanism that downregulates misfolded proteins or those that have finished a programmed task. In the last two decades, neddylation has emerged as a major regulatory pathway for ubiquitination. Central to the neddylation pathway is the amyloid precursor protein (APP)-binding protein APP-BP1, which together with Uba3, plays an analogous role to the ubiquitin-activating enzyme E1 in nedd8 activation. Activated nedd8 covalently modifies and activates a major class of ubiquitin ligases called Cullin-RING ligases (CRLs). New evidence suggests that neddylation also modifies Type-1 transmembrane receptors such as APP. Here we review the functions of neddylation and summarize evidence suggesting that dysfunction of neddylation is involved in Alzheimer's disease.
MIT Department
Massachusetts Institute of Technology. Department of Brain and Cognitive Sciences
Massachusetts Institute of Technology. Department of Materials Science and Engineering
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Creative Commons Attribution
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DOI of Published Version
https://doi.org/10.1111/j.1582-4934.2012.01604.x
