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Título: | SUMO-activated target traps (SATTs) enable the identification of a comprehensive E3-specific SUMO proteome |
Autor: | Salas-Lloret, Daniel; Jansen, Nicolette S.; Nagamalleswari, Easa; Meulen, Coen van der; Gracheva, Ekaterina; Ru, Arnoud H. de; Otte, H. Anne Marie; Veelen, Peter A. van; Pichler, Andrea; Goedhart, Joachim; Vertegaal, Alfred C. O.; González-Prieto, Román CSIC ORCID | Fecha de publicación: | 2-ago-2023 | Editor: | American Association for the Advancement of Science | Citación: | Science Advances 9(31): eadh207 (2023) | Resumen: | Ubiquitin and ubiquitin-like conjugation cascades consist of dedicated E1, E2, and E3 enzymes with E3s providing substrate specificity. Mass spectrometry-based approaches have enabled the identification of more than 6500 SUMO2/3 target proteins. The limited number of SUMO E3s provides the unique opportunity to systematically study E3 substrate wiring. We developed SUMO-activated target traps (SATTs) and systematically identified substrates for eight different SUMO E3s, PIAS1, PIAS2, PIAS3, PIAS4, NSMCE2, ZNF451, LAZSUL (ZNF451-3), and ZMIZ2. SATTs enabled us to identify 427 SUMO1 and 961 SUMO2/3 targets in an E3-specific manner. We found pronounced E3 substrate preference. Quantitative proteomics enabled us to measure substrate specificity of E3s, quantified using the SATT index. Furthermore, we developed the Polar SATTs web-based tool to browse the dataset in an interactive manner. Overall, we uncover E3-to-target wiring of 1388 SUMO substrates, highlighting unique and overlapping sets of substrates for eight different SUMO E3 ligases. | Versión del editor: | http://dx.doi.org/10.1126/sciadv.adh2073 | URI: | http://hdl.handle.net/10261/347049 | DOI: | 10.1126/sciadv.adh2073 | E-ISSN: | 2375-2548 |
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