How to Inactivate Human Ubiquitin E3 Ligases by Mutation
dc.contributor.author | García Bárcena, Cristina ![]() | |
dc.contributor.author | Osinalde Moraleja, Nerea ![]() | |
dc.contributor.author | Ramírez Sánchez, Juan Manuel ![]() | |
dc.contributor.author | Mayor Martínez, Ugo ![]() | |
dc.date.accessioned | 2020-12-23T10:50:05Z | |
dc.date.available | 2020-12-23T10:50:05Z | |
dc.date.issued | 2020-02-04 | |
dc.identifier.citation | Frontiers in Cell and Developmental Biology 8 : (2020) // Article ID 39 | es_ES |
dc.identifier.issn | 2296-634X | |
dc.identifier.uri | http://hdl.handle.net/10810/49229 | |
dc.description.abstract | E3 ubiquitin ligases are the ultimate enzymes involved in the transfer of ubiquitin to substrate proteins, a process that determines the fate of the modified protein. Numerous diseases are caused by defects in the ubiquitin-proteasome machinery, including when the activity of a given E3 ligase is hampered. Thus, inactivation of E3 ligases and the resulting effects at molecular or cellular level have been the focus of many studies during the last few years. For this purpose, site-specific mutation of key residues involved in either protein interaction, substrate recognition or ubiquitin transfer have been reported to successfully inactivate E3 ligases. Nevertheless, it is not always trivial to predict which mutation(s) will block the catalytic activity of a ligase. Here we review over 250 site-specific inactivating mutations that have been carried out in 120 human E3 ubiquitin ligases. We foresee that the information gathered here will be helpful for the design of future experimental strategies. | es_ES |
dc.description.sponsorship | This work was supported by Spanish MINECO (grant SAF2016-76898-P) cofinanced with FEDER funds. JR was funded with a postdoctoral fellowship from the University of the Basque Country (UPV/EHU). | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Frontiers Media | es_ES |
dc.relation | info:eu-repo/grantAgreement/MINECO/SAF2016-76898-P | es_ES |
dc.rights | info:eu-repo/semantics/openAccess | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es/ | * |
dc.subject | ubiquitin | es_ES |
dc.subject | E3 | es_ES |
dc.subject | mutation | es_ES |
dc.subject | ligase | es_ES |
dc.subject | inactivation | es_ES |
dc.subject | ring domain | es_ES |
dc.subject | U-box | es_ES |
dc.subject | down-regulation | es_ES |
dc.subject | protein ligase | es_ES |
dc.subject | C-CBL | es_ES |
dc.subject | finger | es_ES |
dc.subject | degradation | es_ES |
dc.subject | kinase | es_ES |
dc.subject | MDM2 | es_ES |
dc.subject | activation | es_ES |
dc.title | How to Inactivate Human Ubiquitin E3 Ligases by Mutation | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.rights.holder | 2020 Garcia-Barcena, Osinalde, Ramirez and Mayor. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. | es_ES |
dc.rights.holder | Atribución 3.0 España | * |
dc.relation.publisherversion | https://www.frontiersin.org/articles/10.3389/fcell.2020.00039/full | es_ES |
dc.identifier.doi | 10.3389/fcell.2020.00039 | |
dc.departamentoes | Bioquímica y biología molecular | es_ES |
dc.departamentoeu | Biokimika eta biologia molekularra | es_ES |
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Except where otherwise noted, this item's license is described as 2020 Garcia-Barcena, Osinalde, Ramirez and Mayor. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.