Deubiquitinase FAM/USP9X interacts with the E3 ubiquitin ligase SMURF1 protein and protects it from ligase activity-dependent self-degradation
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Xie, Yang, Avello, Monika, Feng, Yan, Schirle, Markus, Bric-Furlong, Eva, Wilson, Christopher, Nathans, Robin, Zhang, Jing, Kirschner, Marc W, Huang, Shih-Min and Cong, Feng (2013) Deubiquitinase FAM/USP9X interacts with the E3 ubiquitin ligase SMURF1 protein and protects it from ligase activity-dependent self-degradation. Journal of Biological Chemistry, 288 (5). pp. 2976-2985. ISSN 0021-9258
Abstract
Background: SMURF1 ubiquitin ligase controls ubiquitination and stability of diverse cellular protein substrates. Results: Deubiquitinase USP9X interacts with SMURF1 and stabilizes SMURF1 through deubiquitination. Conclusion: USP9X is novel regulator of SMURF1 and is required for SMURF1-dependent cellular physiology. Significance: Association between deubiquitinase and ubiquitin ligase may serve as a common strategy to control the cellular protein dynamics through modulating ubiquitin ligase activity. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
| Item Type: | Article |
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| Date Deposited: | 13 Mar 2018 00:45 |
| Last Modified: | 25 Jan 2019 00:46 |
| URI: | https://oak.novartis.com/id/eprint/8465 |