Detailed dissection of UBE3A-mediated DDI1 ubiquitination.

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Date
2019-05-03
Author
Elu Arantzamendi, Nagore ORCID
Osinalde Moraleja, Nerea ORCID
Beaskoetxea Lejarzegi, Javier
Ramírez Sánchez, Juan Manuel ORCID
Lectez, Benoît
Aloria Escolastico, Kerman
Rodríguez Pérez, José Antonio ORCID
Arizmendi Bastarrika, Jesús María ORCID
Mayor Martínez, Ugo ORCID
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Frontiers in Physiology 10 : (2019) // Article ID 534
URI
http://hdl.handle.net/10810/68414
Abstract
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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© 2019 The authors. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY).
Except where otherwise noted, this item's license is described as © 2019 The authors. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY).