Open Access
Article
Expanding PML's functional repertoire through post-translational mechanisms
Jessica N Nichol1,Luca A Petruccelli1,Wilson H Miller Jr1
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
DOI: 10.2741/3380 Volume 14 Issue 6, pp.2293-2306
Published: 01 January 2009
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.

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Jessica N Nichol, Luca A Petruccelli, Wilson H Miller Jr. Expanding PML's functional repertoire through post-translational mechanisms. Frontiers in Bioscience-Landmark. 2009. 14(6); 2293-2306.