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Updated: Mar 16, 2026
06:06
In Vitro Analysis of E3 Ubiquitin Ligase Function
Published on: May 14, 2021
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Ubc13: the Lys63 ubiquitin chain building machine
Curtis D Hodge1, Leo Spyracopoulos1, J N Mark Glover1
1Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada.
Oncotarget
|August 4, 2016
Summary
Ubc13, an E2 enzyme, forms critical Lys63 ubiquitin chains for cellular signaling. This review explores Ubc13
Area of Science:
- Biochemistry and Molecular Biology
- Cellular Signaling
- Drug Discovery
Background:
- Ubc13 is an E2 ubiquitin conjugating enzyme essential for forming lysine 63-linked (Lys63) ubiquitin chains.
- Lys63 ubiquitin chains are crucial signaling molecules in inflammatory and DNA damage response pathways.
- Ubc13 is implicated as a therapeutic target for cancers, drug resistance, inflammation, and viral infections.
Purpose of the Study:
- To provide a comprehensive global review of Ubc13.
- To integrate structural and mechanistic insights with Ubc13's biological functions.
- To assess Ubc13 as a potential therapeutic target by examining its inhibition.
Main Methods:
- Literature review of studies implicating Ubc13 in biological functions.
- Analysis of existing structural data for Ubc13.
- Discussion of natural and chemical inhibition of Ubc13.
Main Results:
- Ubc13 participates with various E3 ligases to generate Lys63 ubiquitin chains.
- Multiple Ubc13 structures reveal a novel activation mechanism involving active site loop conformational changes.
- Ubc13's role in critical cellular pathways highlights its therapeutic potential.
Conclusions:
- Ubc13 is a key enzyme in ubiquitin-dependent signaling pathways.
- Structural insights suggest a unique mechanism for Ubc13 activation.
- Further understanding of Ubc13 is vital for developing targeted therapies for diseases like cancer and chronic inflammation.
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