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Updated: Jun 25, 2026
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Mapping Dysfunctional Protein-Protein Interactions in Disease
Published on: October 24, 2025
Expanding PML's functional repertoire through post-translational mechanisms
Jessica N Nichol1, Luca A Petruccelli, Wilson H Miller
1Montreal Centre for Experimental Therapeutics in Cancer, Sir Mortimer B. Davis Jewish General Hospital, 3755 Chemin de la Cote-Ste-Catherine, Montreal, Quebec, Canada.
Frontiers in Bioscience (Landmark Edition)
|March 11, 2009
Summary
Post-translational modifications like acetylation and ubiquitination expand protein function. This review focuses on how these modifications impact the promyelocytic leukemia (PML) protein and its roles in cellular processes.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Post-translational modifications (PTMs) significantly increase protein functional diversity.
- The promyelocytic leukemia (PML) protein is involved in numerous cellular functions.
- PML protein's activity is regulated by its localization within PML nuclear bodies.
Purpose of the Study:
- To review the expanding knowledge on post-translational modifications of the PML protein.
- To highlight how PTMs regulate the diverse functions of PML.
- To emphasize the importance of PML PTMs in cellular physiology.
Main Methods:
- Literature review of studies on PML protein.
- Analysis of research on acetylation and ubiquitination of PML.
- Synthesis of current understanding of PML PTMs and their effects.
Main Results:
- PML protein undergoes various PTMs, including acetylation and ubiquitination.
- These modifications alter PML protein's stability, localization, and interactions.
- PTMs are crucial for PML's roles in gene regulation, DNA repair, and apoptosis.
Conclusions:
- Post-translational modification is a key regulatory mechanism for PML protein function.
- Understanding PML PTMs is essential for deciphering its complex roles in health and disease.
- Further research into PML modifications will reveal new therapeutic targets.
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