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- W2897066230 abstract "Abstract Covalent modifications of proteins with ubiquitin and ubiquitin-like molecules are instrumental to many biological processes. However, identifying the E3 ligase responsible for these modifications remains a major bottleneck in ubiquitin research. Here, we present an E2-thioester-driven identification (E2~dID) method for the targeted identification of substrates of specific E2 and E3 enzyme pairs. E2~dID exploits the central position of E2-conjugating enzymes in the ubiquitination cascade and provides in vitro generated biotinylated E2~ubiquitin thioester conjugates as the sole source for ubiquitination in extracts. This enables purification and mass spectrometry-based identification of modified proteins under stringent conditions independently of the biological source of the extract. We demonstrate the sensitivity and specificity of E2-dID by identifying and validating substrates of APC/C in human cells. Finally, we perform E2~dID with SUMO in S. cerevisiae , showing that this approach can be easily adapted to other ubiquitin-like modifiers and experimental models." @default.
- W2897066230 created "2018-10-26" @default.
- W2897066230 creator A5001656748 @default.
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- W2897066230 date "2018-11-14" @default.
- W2897066230 modified "2023-09-25" @default.
- W2897066230 title "An E2-ubiquitin thioester-driven approach to identify substrates modified with ubiquitin and ubiquitin-like molecules" @default.
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- W2897066230 doi "https://doi.org/10.1038/s41467-018-07251-5" @default.
- W2897066230 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6235928" @default.
- W2897066230 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30429481" @default.
- W2897066230 hasPublicationYear "2018" @default.
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