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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Detalhes bibliográficos
Autores: Ramírez Sánchez, Juan Manuel, Prieto Agujeta, Gorka, Olazabal Herrero, Ane, Borràs, Eva, Fernandez-Vigo, Elvira, Alduntzin Egizurain, Unai, Osinalde Moraleja, Nerea, Beaskoetxea Lejarzegi, Javier, Lectez, Benoit, Aloria Escolastico, Kerman, Rodríguez Pérez, José Antonio, Paradela, Alberto, Sabidó, Eduard, Muñoz, Javier, Corrales, Fernando, Arizmendi Bastarrika, Jesús María, Mayor Martínez, Ugo
Tipo de documento: artigo
Data de publicação:2021
País:España
Recursos:Universidad del País Vasco
Repositório:Addi. Archivo Digital para la Docencia y la Investigación
OAI Identifier:oai:addi.ehu.eus:10810/51415
Acesso em linha:http://hdl.handle.net/10810/51415
Access Level:Acceso aberto
Palavra-chave:ubiquitination
deubiquitinating enzyme
quantitative proteomics
DUBase
Descrição
Resumo: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.