Редактирование: UBE2N

Ubiquitin-conjugating enzyme E2 N (EC 2.3.2.23) (Bendless-like ubiquitin-conjugating enzyme) (E2 ubiquitin-conjugating enzyme N) (Ubc13) (UbcH13) (Ubiquitin carrier protein N) (Ubiquitin-protein ligase N) [BLU]

==Publications==

{{medline-entry
|title=Aged monkey brains reveal the role of ubiquitin-conjugating enzyme [[UBE2N]] in the synaptosomal accumulation of mutant huntingtin.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/25343992
|abstract=Although misfolded proteins are ubiquitinated and cleared by the proteasome, they can accumulate in synapses in aged neurons to promote synaptic dysfunction in a variety of neurodegenerative diseases, including Huntington's disease (HD), which is caused by polyglutamine expansion in huntingtin. The mechanism behind this aging-related phenomenon is unknown and has been difficult to investigate using animals with short life spans. With brain tissues from longer-lived rhesus monkeys of different ages, we found that aging reduces ubiquitin-proteasomal activity and also increases the level of ubiquitin-conjugating enzyme [[UBE2N]] (Ubc13) in synaptosomes. Synaptosomal fractions from aged monkey brain increase in vitro ubiquitinated huntingtin, whereas depletion of [[UBE2N]] markedly reduces this increase. Overexpressing [[UBE2N]] increases the aggregation of mutant huntingtin, and reducing [[UBE2N]] attenuates huntingtin aggregation in cellular and mouse models of HD. Our studies suggest that increased [[UBE2N]] plays a critical role in the synaptosomal accumulation of mutant huntingtin with age. 
|mesh-terms=* Aging
* Animals
* Brain
* Disease Models, Animal
* Huntington Disease
* Macaca mulatta
* Male
* Mice
* Nerve Tissue Proteins
* Neurons
* Peptides
* Proteasome Endopeptidase Complex
* Proteomics
* Synaptosomes
* Ubiquitin-Conjugating Enzymes

|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4321442
}}