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Updated: Oct 2, 2025

Purification of Ubiquitinated p53 Proteins from Mammalian Cells
Published on: March 21, 2022
Regulation of p53 Function by Formation of Non-Nuclear Heterologous Protein Complexes
Lev Zavileyskiy1, Victoria Bunik1,2,3
1Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, 119991 Moscow, Russia.
The tumor suppressor p53 protein forms complexes outside the nucleus, influencing cellular stress responses and functions. Understanding these p53 complexes offers new therapeutic targets for fine-tuning cellular programs.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- The transcription factor p53 is a crucial stress-response protein.
- p53's functions are modulated by interactions with various proteins.
- p53 is found in multiple cellular compartments beyond the nucleus.
Purpose of the Study:
- To investigate non-nuclear p53 heterologous protein complexes.
- To explore the structural determinants and post-translational modifications of these complexes.
- To elucidate the role of these complexes in p53's intricate functions.
Main Methods:
- Analysis of p53 protein-protein interactions in various cellular compartments.
- Characterization of structural and regulatory aspects of p53 complexes.
- Investigation of p53 complex involvement in cellular stress responses and redox regulation.
Main Results:
- Identified numerous non-nuclear p53 complexes with regulatory and metabolic proteins.
- Demonstrated that some complexes sequester p53 or its partners, while others form upon p53 upregulation.
- Highlighted the role of specific complexes in regulating p53's post-translational modifications and redox sensitivity.
Conclusions:
- Non-nuclear p53 complexes significantly contribute to cellular stress management and p53 regulation.
- Understanding these complexes provides insights into p53's diverse roles.
- Targeting p53 protein-protein interactions could lead to novel therapeutic strategies.
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