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Updated: Jun 4, 2026
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Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta
Published on: December 5, 2019
The cullin-RING ubiquitin-protein ligases
Zhihua Hua1, Richard D Vierstra
1Department of Genetics, University of Wisconsin, Madison, Wisconsin 53706-1574, USA. hua3@wisc.edu
Annual Review of Plant Biology
|March 5, 2011
Summary
Ubiquitin conjugation in plants is complex, involving over 1500 E3 ligases. Cullin-RING ligases (CRLs) are crucial for protein degradation, impacting plant signaling, development, and stress responses.
Area of Science:
- Plant Molecular Biology
- Ubiquitin-Proteasome System
- Plant Signaling
Background:
- Ubiquitin (Ub) posttranslational modification regulates plant protein stability, localization, and function.
- The 26S proteasome degrades ubiquitylated proteins, essential for cellular homeostasis and regulation.
- Plant ubiquitylation is highly complex, with over 1500 potential Ub-protein ligases (E3s).
Purpose of the Study:
- To review the organization, structure, and dynamics of Cullin-RING Ligases (CRLs) in plants.
- To explore the substrates, functions, and evolutionary history of plant CRLs.
- To highlight the critical roles of CRLs in diverse plant biological processes.
Main Methods:
- Review of genetic and genomic studies on plant Ub-protein ligases.
- Analysis of the structural components and assembly of CRLs.
- Compilation of known CRL substrates and their associated pathways.
Main Results:
- CRLs are a polymorphic E3 ligase family in plants, crucial for substrate ubiquitylation.
- CRLs act as sensors for hormones and light, influencing plant signaling pathways.
- CRLs regulate key processes including cell cycle, transcription, stress response, and defense.
Conclusions:
- Plant CRLs exhibit organizational complexity and significant evolutionary divergence.
- CRLs are integral to plant biology, affecting nearly all aspects of plant life.
- Understanding CRLs is vital for deciphering plant growth, development, and environmental interactions.
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