Journal of Biological Chemistry · 1994 · 763 citations · 21 references
Life SciencesBiochemistryMolecular BiologyEnzymologyPost-translational ModificationProtein BiochemistryProtein Complex AssemblyProtein DegradationProtein StructureProtein TurnoverProteolytic EnzymesProteolytic ProcessingProteasome SystemProteasome-mediated DegradationRegulatory SubunitsUbiquitin BindingUbiquitin SystemUbiquitin-mediated DegradationUbiquitin-mediated ProteolysisUbiquitin-proteasome Proteolysis
Ubiquitin‑mediated proteolysis regulates diverse cellular processes, and ubiquitin‑conjugated proteins are degraded by a 26 S proteasome composed of more than 30 subunits. The 50‑kDa subunit 5 of the 26 S proteasome binds ubiquitin‑conjugated proteins, requiring at least four ubiquitin units for efficient association, and thereby selects polyubiquitinated proteins for degradation.
Ubiquitin-mediated proteolysis provides an important mechanism for regulating a variety of cellular processes. Ubiquitin-conjugated proteins are degraded by a 26 S protease that contains more than 30 different subunits. Of these, a single 50-kDa polypeptide, subunit 5, specifically binds ubiquitin-lysozyme conjugates. Binding is inhibited by short polymeric chains of ubiquitin but not by ubiquitin monomers or by lysozyme. In addition, subunit 5 binds free ubiquitin chains with efficient association requiring at least four ubiquitins. Thus, proteins conjugated to polymers of ubiquitin may be selected for degradation by a single subunit of the 26 S protease complex.
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Cyclin is degraded by the ubiquitin pathway
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A Multiubiquitin Chain Is Confined to Specific Lysine in a Targeted Short-Lived Protein
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