title: Regulation of catalytic activities of HECT ubiquitin ligases.
abstract: Studies in yeast and mammalian cells over the past decade have shown that HECT domain ubiquitin ligases (HECT E3 enzymes) are involved in diverse physiological pathways. Many substrates of specific HECT E3s have been identified, as well as many adaptor proteins that aid in defining substrate specificity or intra-cellular localization of HECT E3s. Here we review some recently discovered mechanisms for regulation of the catalytic activities of HECT E3s, including regulation at the level of E2 recruitment, phosphorylation-dependent relief of inhibitory intra-molecular interactions, and regulation by association with a deubiquitinating enzyme.
authors.affiliation: Institute for Cellular and Molecular Biology, Section of Molecular Genetics and Microbiology, University of Texas at Austin, Austin, TX 78712, USA.
authors.forename: Younghoon
authors.initials: Y
authors.lastname: Kee
authors.forename: Jon M
authors.initials: JM
authors.lastname: Huibregtse
mesh_terms: D000818:Animals; D002384:Catalysis; D056827:Endosomal Sorting Complexes Required for Transport; D006801:Humans; D012097:Repressor Proteins / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins / Q000502:physiology; D025801:Ubiquitin / Q000378:metabolism; D043743:Ubiquitin-Protein Ligase Complexes / Q000502:physiology; D044767:Ubiquitin-Protein Ligases / Q000502:physiology*
chemical_list: D056827:Endosomal Sorting Complexes Required for Transport; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D025801:Ubiquitin; D043743:Ubiquitin-Protein Ligase Complexes; C432966:ITCH protein, human; C471641:SMURF2 protein, human; D044767:Ubiquitin-Protein Ligases; C469287:RSP5 protein, S cerevisiae