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Kudriaeva AA, Livneh I, Baranov MS, et al. In-depth characterization of ubiquitin turnover in mammalian cells by fluorescence tracking. Cell Chem Biol. 2021;28(8):1192-1205.e9doi: 10.1016/j.chembiol.2021.02.009.
Kudriaeva, A. A., Livneh, I., Baranov, M. S., Ziganshin, R. H., Tupikin, A. E., Zaitseva, S. O., Kabilov, M. R., Ciechanover, A., & Belogurov, A. A. (2021). In-depth characterization of ubiquitin turnover in mammalian cells by fluorescence tracking. Cell chemical biology, 28(8), 1192-1205.e9. https://doi.org/10.1016/j.chembiol.2021.02.009
Kudriaeva, Anna A, et al. "In-depth characterization of ubiquitin turnover in mammalian cells by fluorescence tracking." Cell chemical biology vol. 28,8 (2021): 1192-1205.e9. doi: https://doi.org/10.1016/j.chembiol.2021.02.009
Kudriaeva AA, Livneh I, Baranov MS, Ziganshin RH, Tupikin AE, Zaitseva SO, Kabilov MR, Ciechanover A, Belogurov AA. In-depth characterization of ubiquitin turnover in mammalian cells by fluorescence tracking. Cell Chem Biol. 2021 Aug 19;28(8):1192-1205.e9. doi: 10.1016/j.chembiol.2021.02.009. Epub 2021 Mar 05. PMID: 33675681.
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Cell Chem Biol. 2021 Aug 19;28(8):1192-1205.e9. doi: 10.1016/j.chembiol.2021.02.009. Epub 2021 Mar 05.

In-depth characterization of ubiquitin turnover in mammalian cells by fluorescence tracking.

Cell chemical biology

Anna A Kudriaeva, Ido Livneh, Mikhail S Baranov, Rustam H Ziganshin, Alexey E Tupikin, Snizhana O Zaitseva, Marsel R Kabilov, Aaron Ciechanover, Alexey A Belogurov

Affiliations

  1. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya 16/10, 117997 Moscow, Russian Federation.
  2. Technion Integrated Cancer Center, The Rappaport Faculty of Medicine and Research Institute, Technion-Israel Institute of Technology, 3109602 Haifa, Israel.
  3. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya 16/10, 117997 Moscow, Russian Federation; Pirogov Russian National Research Medical University, Ostrovitianov 1, 117997 Moscow, Russian Federation.
  4. Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, Lavrentieva 8, 630090 Novosibirsk, Russian Federation.
  5. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya 16/10, 117997 Moscow, Russian Federation; Lomonosov Moscow State University, Leninskie Gory, 119991 Moscow, Russian Federation. Electronic address: [email protected].

PMID: 33675681 DOI: 10.1016/j.chembiol.2021.02.009

Abstract

Despite almost 40 years having passed from the initial discovery of ubiquitin (Ub), fundamental questions related to its intracellular metabolism are still enigmatic. Here we utilized fluorescent tracking for monitoring ubiquitin turnover in mammalian cells, resulting in obtaining qualitatively new data. In the present study we report (1) short Ub half-life estimated as 4 h; (2) for a median of six Ub molecules per substrate as a dynamic equilibrium between Ub ligases and deubiquitinated enzymes (DUBs); (3) loss on average of one Ub molecule per four acts of engagement of polyubiquitinated substrate by the proteasome; (4) direct correlation between incorporation of Ub into the distinct type of chains and Ub half-life; and (5) critical influence of the single lysine residue K27 on the stability of the whole Ub molecule. Concluding, our data provide a comprehensive understanding of ubiquitin-proteasome system dynamics on the previously unreachable state of the art.

Copyright © 2021 Elsevier Ltd. All rights reserved.

Keywords: half-life; metabolism; polyubiquitin chain length; proteasome; resorufin ligase; stability; ubiquitin

Conflict of interest statement

Declaration of interests The authors declare no competing interests.

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