Mechanisms for regulating deubiquitinating enzymes

Authors

  • Cynthia Wolberger

    Corresponding author
    1. Department of Biophysics and Biophysical Chemistry and the Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland
    • Correspondence to: Cynthia Wolberger, Department of Biophysics and Biophysical Chemistry and the Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, 725 N. Wolfe St., Baltimore, MD 21205. E-mail: cwolberg@jhmi.edu

    Search for more papers by this author

  • Cynthia Wolberger is the co-recipient of the Protein Society 2013 Dorothy Crowfoot Hodgkin Award.

Abstract

Ubiquitination is a reversible post-translational modification that plays a dynamic role in regulating most eukaryotic processes. Deubiquitinating enzymes (DUBs), which hydrolyze the isopeptide or peptide linkages joining ubiquitin to substrate lysines or N-termini, therefore play a key role in ubiquitin signaling. Cells employ multiple mechanisms to regulate DUB activity and thus ensure the appropriate biological response. Recent structural studies have shed light on several different mechanisms by which DUB activity and specificity is regulated.

Ancillary