Twists and turns in ubiquitin-like protein conjugation cascades

Authors

  • Brenda A. Schulman

    Corresponding author
    1. Department of Structural Biology and Tumor Cell Biology and Howard Hughes Medical Institute, St. Jude Children's Research Hospital, Memphis, Tennessee 38105
    • Department of Structural Biology and Tumor Cell Biology and Howard Hughes Medical Institute, St. Jude Children's Research Hospital, MS #311, 262 Danny Thomas Place, Memphis, TN 38105
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  • Dr. Schulman is the co-recipient of the 2011 Dorothy Crowfoot Hodgkin Award granted in recognition of exceptional contributions in protein science which profoundly influence our understanding of biology.

Abstract

Post-translational modification by ubiquitin-like proteins (UBLs) is a predominant eukaryotic regulatory mechanism. The vast reach of this form of regulation extends to virtually all eukaryotic processes that involve proteins. UBL modifications play critical roles in controlling the cell cycle, transcription, DNA repair, stress responses, signaling, immunity, plant growth, embryogenesis, circadian rhythms, and a plethora of other pathways. UBLs dynamically modulate target protein properties including enzymatic activity, conformation, half-life, subcellular localization, and intermolecular interactions. Moreover, the enzymatic process of UBL ligation to proteins is itself dynamic, with the UBL moving between multiple enzyme active sites and ultimately to a target. This review highlights our work on how the dynamic conformations of selected enzymes catalyzing UBL ligation help mediate this fascinating form of protein regulation.

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