title: Molecular mechanisms of ubiquitin-dependent membrane traffic.
abstract: Over the past 14 years, ubiquitination has emerged as a centrally important mechanism governing the subcellular trafficking of proteins. Ubiquitination, interaction with sorting factors that contain ubiquitin-binding domains, and deubiquitination govern the itineraries of cargo proteins that include yeast carboxypeptidase S, the epithelial sodium channel ENaC, and epidermal growth factor receptor. The molecular structures and mechanisms of the paradigmatic HECT and RING domain ubiquitin ligases, of JAMM- and USP-domain-deubiquitinating enzymes, and of numerous ubiquitin-binding domains involved in these pathways have been worked out in recent years and are described.
authors.affiliation: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0580, USA. hurley@helix.nih.gov
authors.forename: James H
authors.initials: JH
authors.lastname: Hurley
authors.forename: Harald
authors.initials: H
authors.lastname: Stenmark
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000737:chemistry* / Q000378:metabolism*; D003198:Computer Simulation; D006801:Humans; D008954:Models, Biological; D008956:Models, Chemical; D021381:Protein Transport / Q000502:physiology*; D025801:Ubiquitin / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D025801:Ubiquitin