title: Degradation of proteins by the ubiquitin-mediated proteolytic pathway.
abstract: Degradation of a protein by the ubiquitin system involves two distinct processes. In the first step, ubiquitin is covalently linked in an ATP-dependent mode to the protein substrate. The protein moiety of the conjugate is then degraded by a specific protease into free amino acids, resulting in the release of free and reutilizable ubiquitin. This process also requires energy. In this review we will briefly summarize our current knowledge of the role of the ubiquitin system in protein turnover and discuss in detail the mechanism involved in selection of substrates for conjugation and in degradation of ubiquitin-conjugated proteins.
authors.affiliation: Department of Biochemistry, Rappaport Institute for Research in Medical Sciences, Technion-Israel Institute of Technology, Haifa.
authors.forename: A
authors.initials: A
authors.lastname: Ciechanover
authors.forename: H
authors.initials: H
authors.lastname: Gonen
authors.forename: S
authors.initials: S
authors.lastname: Elias
authors.forename: A
authors.initials: A
authors.lastname: Mayer
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D066298:In Vitro Techniques; D010447:Peptide Hydrolases / Q000378:metabolism; D021382:Protein Sorting Signals / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D013379:Substrate Specificity; D014452:Ubiquitins / Q000378:metabolism*
chemical_list: D021382:Protein Sorting Signals; D011506:Proteins; D014452:Ubiquitins; D000255:Adenosine Triphosphate; D010447:Peptide Hydrolases