dc.contributor.author | Halim, Vincentius A. | |
dc.contributor.author | García Santisteban, Iraia ![ORCID](/themes/Mirage2//images/orcid_16x16.png) | |
dc.contributor.author | Warmerdam, Daniel O | |
dc.contributor.author | Van den Broek, Bram | |
dc.contributor.author | Heck, Albert J. R. | |
dc.contributor.author | Mohammed, Shabaz | |
dc.contributor.author | Medema, René H. | |
dc.date.accessioned | 2019-01-16T09:13:22Z | |
dc.date.available | 2019-01-16T09:13:22Z | |
dc.date.issued | 2018-12 | |
dc.identifier.citation | Molecular & Cellular Proteomics 17(12) : 2297-2308 (2018) | es_ES |
dc.identifier.issn | 1535-9476 | |
dc.identifier.issn | 1535-9484 | |
dc.identifier.uri | http://hdl.handle.net/10810/30895 | |
dc.description.abstract | Protein posttranslational modifications (PTMs) play a central role in the DNA damage response. In particular, protein phosphorylation and ubiquitination have been shown to be essential in the signaling cascade that coordinates break repair with cell cycle progression. Here, we performed whole-cell quantitative proteomics to identify global changes in protein ubiquitination that are induced by DNA double-strand breaks. In total, we quantified more than 9,400 ubiquitin sites and found that the relative abundance of similar to 10% of these sites was altered in response to DNA double-strand breaks. Interestingly, a large proportion of ribosomal proteins, including those from the 40S as well as the 60S subunit, were ubiquitinated in response to DNA damage. In parallel, we discovered that DNA damage leads to the inhibition of ribosome function. Taken together, these data uncover the ribosome as a major target of the DNA damage response. | es_ES |
dc.description.sponsorship | This work is funded by a TOP-GO grant from the Netherlands Organization for Scientific Research (NWO ZonMW 912100651 to R.H.M., S.M., and V.A.H.). I.G.S. was supported with a postdoctoral fellowship from the Basque Country Government (Spain). We thank Christian Frese and Teck Yew Low for fruitful discussions. We also thank Teck Yew Low for submitting the raw files and annotated spectra to PRIDE. We thank Fabricio Loayza-Puch for his technical help with the sucrose gradients. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | American Society for Biochemistry and Molecular Biology | es_ES |
dc.rights | info:eu-repo/semantics/openAccess | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es/ | * |
dc.subject | polo-like kinase-1 | es_ES |
dc.subject | messenger-rnas | es_ES |
dc.subject | p53 | es_ES |
dc.subject | recovery | es_ES |
dc.subject | repair | es_ES |
dc.subject | ubiquitylation | es_ES |
dc.subject | identification | es_ES |
dc.subject | recruitment | es_ES |
dc.subject | claspin | es_ES |
dc.subject | quantification | es_ES |
dc.title | Doxorubicin-induced DNA Damage Causes Extensive Ubiquitination of Ribosomal Proteins Associated with a Decrease in Protein Translation | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.rights.holder | Final version open access under the terms of the Creative Commons CC-BY license | es_ES |
dc.rights.holder | Atribución 3.0 España | * |
dc.relation.publisherversion | http://www.mcponline.org/content/17/12/2297 | es_ES |
dc.identifier.doi | 10.1074/mcp.RA118.000652 | |
dc.departamentoes | Genética, antropología física y fisiología animal | es_ES |
dc.departamentoeu | Genetika,antropologia fisikoa eta animalien fisiologia | es_ES |