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Updated: Aug 2, 2025

Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations
Published on: November 7, 2019
Cell-Permeable Ubiquitin and Histone Tools for Studying Post-translational Modifications
Jia-Hui Tang1, Qing-Yao Shu2, Yan-Yan Guo2
1School of Food and Biological Engineering, Hefei University of Technology, Hefei, Anhui 230009, China.
Synthetic protein tools for post-translational modifications (PTMs) are now cell-permeable, enabling enzyme activity and proteome studies in live cells. This advances understanding of biological processes regulated by PTMs.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Protein post-translational modifications (PTMs) are crucial regulators of eukaryotic cellular processes.
- Synthetic PTM protein tools are established for detecting enzyme activity and identifying protein interactors in cell lysates.
- Investigating PTM enzymes and their interactomes in live cells presents unique challenges.
Purpose of the Study:
- To introduce cell-permeable synthetic PTM protein tools for live-cell applications.
- To discuss methodologies for synthesizing these cell-penetrating tools.
- To explore future perspectives in the field of live-cell PTM analysis.
Main Methods:
- Development of cell-penetrating techniques for PTM protein tools.
- Synthesis strategies for creating cell-permeable PTM protein probes.
- Application of these tools for studying enzyme activity and protein interactions in intact cells.
Main Results:
- Demonstration of successful delivery of synthetic PTM protein tools into live eukaryotic cells.
- Validation of the tools' ability to detect enzyme activity and identify interacting proteins within the cellular environment.
- Establishment of a novel approach for real-time PTM-related biological process analysis.
Conclusions:
- Cell-permeable PTM protein tools represent a significant advancement for studying biological processes in live cells.
- These tools facilitate the investigation of enzyme dynamics and proteome interactions with unprecedented spatial and temporal resolution.
- Future research directions include refining tool design and expanding their application to diverse biological systems.
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