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A substrate-trapping strategy to find E3 ubiquitin ligase substrates identifies Parkin and TRIM28 targets

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Title: A substrate-trapping strategy to find E3 ubiquitin ligase substrates identifies Parkin and TRIM28 targets
Authors: Watanabe, Masashi Browse this author →KAKEN DB
Saeki, Yasushi Browse this author
Takahashi, Hidehisa Browse this author →KAKEN DB
Ohtake, Fumiaki Browse this author
Yoshida, Yukiko Browse this author
Kasuga, Yusuke Browse this author
Kondo, Takeshi Browse this author
Yaguchi, Hiroaki Browse this author
Suzuki, Masanobu Browse this author
Ishida, Hiroki Browse this author
Tanaka, Keiji Browse this author
Hatakeyama, Shigetsugu Browse this author →KAKEN DB
Issue Date: 20-Oct-2020
Publisher: Nature Research
Journal Title: Communications biology
Volume: 3
Issue: 1
Start Page: 592
Publisher DOI: 10.1038/s42003-020-01328-y
Abstract: The identification of true substrates of an E3 ligase is biologically important but biochemically difficult. In recent years, several techniques for identifying substrates have been developed, but these approaches cannot exclude indirect ubiquitination or have other limitations. Here we develop an E3 ligase substrate-trapping strategy by fusing a tandem ubiquitin-binding entity (TUBE) with an anti-ubiquitin remnant antibody to effectively identify ubiquitinated substrates. We apply this method to one of the RBR-type ligases, Parkin, and to one of the RING-type ligases, TRIM28, and identify previously unknown substrates for TRIM28 including cyclin A2 and TFIIB. Furthermore, we find that TRIM28 promotes cyclin A2 ubiquitination and degradation at the G1/S phase and suppresses premature entry into S phase. Taken together, the results indicate that this method is a powerful tool for comprehensively identifying substrates of E3 ligases. Watanabe et al. combine two previously developed strategies to identify E3 ubiquitin ligase substrates into a method, TR-TUBE that is subsequently used to identify substrates of the Parkin and TRIM28 ligases. They identify known substrates, validating the utility of the approach, and find that TRIM28 targets Cyclin A and TFIIB for degradation.
Rights: http://creativecommons.org/licenses/by/4.0/
Type: article
URI: http://hdl.handle.net/2115/80000
Appears in Collections:医学院・医学研究院 (Graduate School of Medicine / Faculty of Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

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