title: Mechanisms for regulating deubiquitinating enzymes.
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.
authors.affiliation: Department of Biophysics and Biophysical Chemistry and the Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland, 21205.
authors.forename: Cynthia
authors.initials: C
authors.lastname: Wolberger
mesh_terms: D006801:Humans; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D015398:Signal Transduction; D025801:Ubiquitin / Q000737:chemistry / Q000378:metabolism; D064570:Ubiquitin-Specific Proteases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: D010455:Peptides; D025801:Ubiquitin; D064570:Ubiquitin-Specific Proteases
keywords: DUB; UBL; deubiquitinating enzymes; ubiquitin