[Frontiers in Bioscience 14, 2293-2306, January 1, 2009]

Expanding PML's functional repertoire through post-translational mechanisms

Jessica N. Nichol1, Luca A. Petruccelli1, Wilson H. Miller, Jr.1

1Montreal Centre for Experimental Therapeutics in Cancer, Sir Mortimer B. Davis Jewish General Hospital, 3755 Chemin de la Cote-Ste-Catherine, Montreal, Quebec, Canada

TABLE OF CONTENTS

1. Abstract
2. Introduction
3. SUMOylation of PML
3.1. SUMO conjugation pathway
3.2. Nuclear body assembly
3.3. Transcirptional role
3.4. Viral attack
3.5. Cell cycle
4. PML phosphorylation
4.1. Tumor suppression
4.2. DNA damage
4.3. SUMO crosstalk
5. PML/RARalpha
5.1. ISG15
5.2. SUMOylation
5.3. Phosphorylation
6. Concluding remarks
7. Acknowledgement
8. References

1. ABSTRACT

Post-translational modifications, such as acetylation and ubiquitination, can greatly expand the functionality of a particular protein. The promyelocytic leukemia (PML) protein is a functionally promiscuous protein with proposed roles in many cellular processes. Its cellular headquarters are the macromolecular structures termed PML nuclear bodies. Post-translational modification of PML is emerging as a defining feature of this protein that regulates its physiological consequences. This review will highlight the expansion of our knowledge about the post-translational modifications of PML.