title: Rad23 and Rpn10: perennial wallflowers join the melee.
abstract: Substrate ubiquitination is highly regulated; by contrast, substrate targeting to the proteasome has been considered a stochastic process that is mediated primarily by high-affinity interaction with multi-ubiquitin chains. However, recent findings have shown that substrate recognition by the proteasome is also regulated, and requires Rad23, Dsk2 and Rpn10. These studies suggest that the engagement of protein ubiquitination and translocation with degradation by the proteasome is coordinated by a series of regulated events.
authors.affiliation: Robert Wood Johnson Medical School, Department of Biochemistry, 683 Hoes Lane, Piscataway, NJ 08854, USA. maduraki@umdnj.edu
authors.forename: Kiran
authors.initials: K
authors.lastname: Madura
mesh_terms: D002352:Carrier Proteins / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D005544:Forecasting; D005656:Fungal Proteins / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins; D025801:Ubiquitin / Q000378:metabolism
chemical_list: D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; C122019:RPN10 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D025801:Ubiquitin; D046988:Proteasome Endopeptidase Complex