A proteomic approach for systematic mapping of substrates of human deubiquitinating enzymes

The human genome contains nearly 100 deubiquitinating enzymes (DUBs) responsible for removing ubiquitin moieties from a large variety of substrates. Which DUBs are responsible for targeting which substrates remain mostly unknown. Here we implement the bioUb approach to identify DUB substrates in a s...

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Detalles Bibliográficos
Autores: Ramirez, Juanma, Prieto, Gorka, Olazabal-Herrero, Anne, Borràs, Eva, Fernandez-Vigo, Elvira, Alduntzin, Unai, Osinalde, Nerea, Beaskoetxea, Javier, Lectez, Benoit, Aloria, Kerman, Rodríguez, José Antonio, Paradela, Alberto, Sabidó Aguadé, Eduard, 1981-, Muñoz, Javier, Corrales, Fernando, Arizmendi, Jesús M., Mayor, Ugo
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2021
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:10230/49053
Acceso en línea:http://hdl.handle.net/10230/49053
http://dx.doi.org/10.3390/ijms22094851
Access Level:acceso abierto
Palabra clave:DUBase
Deubiquitinating enzyme
Quantitative proteomics
Ubiquitination
Descripción
Sumario:The human genome contains nearly 100 deubiquitinating enzymes (DUBs) responsible for removing ubiquitin moieties from a large variety of substrates. Which DUBs are responsible for targeting which substrates remain mostly unknown. Here we implement the bioUb approach to identify DUB substrates in a systematic manner, combining gene silencing and proteomics analyses. Silencing of individual DUB enzymes is used to reduce their ubiquitin deconjugating activity, leading to an increase of the ubiquitination of their substrates, which can then be isolated and identified. We report here quantitative proteomic data of the putative substrates of 5 human DUBs. Furthermore, we have built a novel interactive database of DUB substrates to provide easy access to our data and collect DUB proteome data from other groups as a reference resource in the DUB substrates research field.