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In Vitro Analysis of E3 Ubiquitin Ligase Function
Published on: May 14, 2021
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Posing the APC/C E3 Ubiquitin Ligase to Orchestrate Cell Division
Edmond R Watson1, Nicholas G Brown2, Jan-Michael Peters3
1Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, 82152, Germany.
Trends in Cell Biology
|November 29, 2018
Summary
The anaphase promoting complex/cyclosome (APC/C) is a dynamic E3 ligase controlling cell division. Its structure changes upon binding partners, enabling precise ubiquitylation for cell cycle regulation.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- The anaphase promoting complex/cyclosome (APC/C) is a crucial E3 ubiquitin ligase.
- It regulates key cell cycle transitions, including mitosis and nonmitotic pathways.
- Recent discoveries highlight the dynamic nature of its catalytic subunits, cullin and RING proteins.
Purpose of the Study:
- To review the structural mechanisms governing APC/C regulation.
- To elucidate how coactivators, E2 enzymes, and inhibitors interact with the APC/C.
- To understand how structural dynamics dictate APC/C function in ubiquitylation.
Main Methods:
- Structural biology analysis
- Review of existing literature on APC/C interactions
- Analysis of protein dynamics and conformational changes
Main Results:
- APC/C engages coactivators, E2 ubiquitin-conjugating enzymes, and inhibitors at multiple sites, including the cullin-RING catalytic core.
- The mobility of coactivators and cullin-RING domains allows APC/C to adopt distinct conformations.
- These conformational changes are critical for specifying different ubiquitylation functions.
Conclusions:
- APC/C functions as a dynamic, multifunctional molecular machine, not merely an interaction hub.
- Binding partners remodel APC/C structure to achieve temporal ubiquitylation.
- This remodeling is essential for regulating cell division and other cellular processes.
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