IMR Press / FBL / Volume 14 / Issue 6 / DOI: 10.2741/3380

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
Expanding PML's functional repertoire through post-translational mechanisms
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1 Montreal Centre for Experimental Therapeutics in Cancer, Sir Mortimer B. Davis Jewish General Hospital, 3755 Chemin de la Cote-Ste-Catherine, Montreal, Quebec, Canada
Academic Editor:Katherine Borden
Front. Biosci. (Landmark Ed) 2009, 14(6), 2293–2306;
Published: 1 January 2009

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.

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