Display Settings:

Format

Send to:

Choose Destination
    Front Biosci. 2009 Jan 1;14:2293-306.

    Expanding PML's functional repertoire through post-translational mechanisms.

    Source

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

    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.

    PMID:
    19273202
    [PubMed - indexed for MEDLINE]

      Supplemental Content

      Icon for Frontiers in Bioscience

      Save items

      loading

      Recent activity

      Your browsing activity is empty.

      Activity recording is turned off.

      Turn recording back on

      See more...
      Write to the Help Desk