Dysfunction of the ubiquitin ligase E3A Ube3A/E6-AP contributes to synaptic pathology in Alzheimer’s disease View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2019-12

AUTHORS

Markel Olabarria, Silvia Pasini, Carlo Corona, Pablo Robador, Cheng Song, Hardik Patel, Roger Lefort

ABSTRACT

Synaptic dysfunction and synapse loss are prominent features in Alzheimer's disease. Members of the Rho-family of guanosine triphosphatases, specifically RhoA, and the synaptic protein Arc are implicated in these pathogenic processes. They share a common regulatory molecule, the E3 ligase Ube3A/E6-AP. Here, we show that Ube3A is reduced in an Alzheimer's disease mouse model, Tg2576 mouse, which overexpresses human APP695 carrying the Swedish mutation, and accumulates Aβ in the brain. Depletion of Ube3A precedes the age-dependent behavioral deficits and loss of dendritic spines in these mice, and results from a decrease in solubility following phosphorylation by c-Abl, after Aβ exposure. Loss of Ube3A triggers the accumulation of Arc and Ephexin-5, driving internalization of GluR1, and activation of RhoA, respectively, culminating in pruning of synapses, which is blocked by restoring Ube3A. Taken together, our results place Ube3A as a critical player in Alzheimer's disease pathogenesis, and as a potential therapeutic target. More... »

PAGES

111

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s42003-019-0350-5

DOI

http://dx.doi.org/10.1038/s42003-019-0350-5

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1112942994

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30937395


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