Work

Molecular Mechanisms of Ubiquitin-Dependent Membrane Traffic

Year: 2011

Type: review

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.

Source: Annual Review of Biophysics

DOI: 10.1146/annurev-biophys-042910-155404

Authors: James H. Hurley, Harald Stenmark

Institutions: National Institutes of Health, National Institute of Diabetes and Digestive and Kidney Diseases, Oslo University Hospital, University of Oslo

Language: English

Topic: Ubiquitin and proteasome pathways

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: Norges Forskningsråd, National Institutes of Health, National Institute of Diabetes and Digestive and Kidney Diseases

Award: Structural and Functional Studies of Ubiquitin Binding Domains