期刊
FRONTIERS IN PHYSIOLOGY
卷 10, 期 -, 页码 -出版社
FRONTIERS MEDIA SA
DOI: 10.3389/fphys.2019.00534
关键词
UBE3A; ubiquitin E3 ligase; Angelman syndrome; proteasome; mass-spectrometry; GFP pull-down
类别
资金
- March of Dimes [1-FY15-339]
- Spanish MINECO [SAF2016-76898-P]
- FEDER funds
- grant PRB3 [IPT17/0019 - ISCIII-SGEFI / ERDF]
- Fondation Jerome Lejeune grant [1381-MU2015A]
The ubiquitin E3 ligase UBE3A has been widely reported to interact with the proteasome, but it is still unclear how this enzyme regulates by ubiquitination the different proteasomal subunits. The proteasome receptor DDI1 has been identified both in Drosophila photoreceptor neurons and in human neuroblastoma cells in culture as a direct substrate of UBE3A. Here, we further characterize this regulation, by identifying the UBE3A-dependent ubiquitination sites and ubiquitin chains formed on DDI1. Additionally, we found one deubiquitinating enzyme that is capable of reversing the action of UBE3A on DDI1. The complete characterization of the ubiquitination pathway of an UBE3A substrate is important due to the role of this E3 ligase in rare neurological disorders as Angelman syndrome.
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