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Updated: May 21, 2025

Purification of Ubiquitinated p53 Proteins from Mammalian Cells

Purification of Ubiquitinated p53 Proteins from Mammalian Cells

Published on: March 21, 2022

Designer polyQ fusion proteins sequester USP7/HDM2 for modulating P53 functionality.

Xiang-Le Zhang^1,2, Hong-Wei Yue^1,2, Ya-Jun Liu^1,2

¹Key Laboratory of RNA Innovation, Science and Engineering, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai 200031, P.R. China.

|March 19, 2025

Summary

This summary is machine-generated.

Engineered polyQ fusion proteins can sequester USP7 and HDM2, reactivating P53 signaling. This strategy shows therapeutic potential for cancer by modulating P53 stability and function.

Keywords:

Biochemistry Cancer Protein structure aspects

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Yeast As a Chassis for Developing Functional Assays to Study Human P53

Yeast As a Chassis for Developing Functional Assays to Study Human P53

Published on: August 4, 2019

Area of Science:

Oncology
Molecular Biology
Protein Engineering

Background:

Overexpression of USP7 and HDM2 inactivates P53 signaling in tumor cells, promoting cancer progression.
Targeting USP7 and HDM2 to restore P53 function is a significant challenge in cancer therapy.

Purpose of the Study:

To engineer polyQ fusion proteins for specific sequestration of USP7 and HDM2.
To modulate P53 stability and functionality through targeted protein aggregation.

Main Methods:

Design and application of polyQ sequences fused with target-interacting peptides.
Engineering of designer fusion proteins, such as Atx793Q-N172-IRF and Atx793Q-N172-PMI.
Analysis of P53 level modulation and downstream gene expression.

Main Results:

The fusion protein Atx793Q-N172-IRF sequesters USP7 and/or HDM2, increasing P53 levels, with effects dependent on IRF repeats.
Depletion of USP7 availability by fusion proteins plays a dual role in controlling P53 stability.
Direct sequestration of HDM2 by Atx793Q-N172-PMI significantly reduces soluble HDM2, increasing P53 levels and up-regulating downstream gene expression.

Conclusions:

The polyQ-fusion strategy is a feasible approach to modulate P53 stability and functionality.
Engineered polyQ fusion proteins demonstrate therapeutic potential for cancer treatment by targeting USP7 and HDM2.