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Updated: May 19, 2026
10:55
Purification of Ubiquitinated p53 Proteins from Mammalian Cells
Published on: March 21, 2022
UHRF2, another E3 ubiquitin ligase for p53
Lu Bai1, Xiaohui Wang, Fangmin Jin
1Department of Cell Biology and Medical Genetics, Chongqing Medical University, Chongqing, China.
Biochemical and Biophysical Research Communications
|August 21, 2012
Summary
Ubiquitin-like with PHD and ring finger domains 2 (UHRF2) ligase targets tumor suppressor p53 for ubiquitination. This discovery suggests a new cell proliferation pathway involving UHRF2 and p53 in cell cycle regulation.
Area of Science:
- Molecular Biology
- Epigenetics
- Cell Biology
Background:
- UHRF2 (ubiquitin-like with PHD and ring finger domains 2) is a nuclear E3 ubiquitin ligase.
- UHRF2 plays roles in cell cycle control and epigenetic regulation.
- It interacts with cyclins, CDKs, pRb, DNMTs, G9a, HDAC1, and histone modifications.
Purpose of the Study:
- To investigate the interaction between UHRF2 and tumor suppressor protein p53.
- To determine if UHRF2 ubiquitinates p53.
Main Methods:
- In vivo and in vitro ubiquitination assays were performed.
- Protein interaction studies were conducted.
Main Results:
- UHRF2 was found to associate with p53.
- UHRF2 was demonstrated to ubiquitinate p53 both in vivo and in vitro.
Conclusions:
- UHRF2 directly ubiquitinates the tumor suppressor p53.
- This interaction suggests a novel signaling pathway involving UHRF2 and p53 in cell proliferation and cell cycle regulation.
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