Journal
ANNUAL REVIEW OF BIOPHYSICS, VOL 40
Volume 40, Issue -, Pages 119-142Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biophys-042910-155404
Keywords
lysosome; EGF receptor; ENaC; RING domain; HECT domain; JAMM domain; ubiquitin-binding domain
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Funding
- Intramural NIH HHS [ZIA DK036126-05] Funding Source: Medline
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [ZIADK036126] Funding Source: NIH RePORTER
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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.
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