Document Type
Article
Publication Date
5-23-2016
Abstract
BACKGROUND: Cullin-RING E3 ubiquitin ligase complexes play a central role in targeting cellular proteins for ubiquitination-dependent protein turnover through 26S proteasome. Cullin-2 is a member of the Cullin family, and it serves as a scaffold protein for Elongin B and C, Rbx1 and various substrate recognition receptors to form E3 ubiquitin ligases.
MAIN BODY OF THE ABSTRACT: First, the composition, structure and the regulation of Cullin-2 based E3 ubiquitin ligases were introduced. Then the targets, the biological functions of complexes that use VHL, Lrr-1, Fem1b, Prame, Zyg-11, BAF250, Rack1 as substrate targeting subunits were described, and their involvement in diseases was discussed. A small molecule inhibitor of Cullins as a potential anti-cancer drug was introduced. Furthermore, proteins with VHL box that might bind to Cullin-2 were described. Finally, how different viral proteins form E3 ubiquitin ligase complexes with Cullin-2 to counter host viral defense were explained.
CONCLUSIONS: Cullin-2 based E3 ubiquitin ligases, using many different substrate recognition receptors, recognize a number of substrates and regulate their protein stability. These complexes play critical roles in biological processes and diseases such as cancer, germline differentiation and viral defense. Through the better understanding of their biology, we can devise and develop new therapeutic strategies to treat cancers, inherited diseases and viral infections.
Recommended Citation
Cai, Weijia and Yang, Haifeng, "The structure and regulation of Cullin 2 based E3 ubiquitin ligases and their biological functions." (2016). Department of Pathology, Anatomy, and Cell Biology Faculty Papers. Paper 191.
https://jdc.jefferson.edu/pacbfp/191
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.
PubMed ID
27222660
Comments
This article has been peer reviewed. It was published in: Cell Division.
Volume 11, Issue 1, 23 May 2016, Article number 7.
The published version is available at DOI: 10.1186/s13008-016-0020-7
Copyright © The Author(s). 2016
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