2008
An emerging role for thioester‐linked polyubiquitin chains in protein degradation
Ravid T, Hochstrasser M. An emerging role for thioester‐linked polyubiquitin chains in protein degradation. The FASEB Journal 2008, 22: 605.7-605.7. DOI: 10.1096/fasebj.22.1_supplement.605.7.Peer-Reviewed Original ResearchPolyubiquitin chainsE2 enzymeCatalytic cysteineUbiquitin chainsProtein quality control systemUndergoes proteasomal degradationUbiquitin chain assemblyER membraneE3 ligaseTransmembrane proteinProteasomal degradationDegradation signalProtein degradationLysine side chainsQuality control systemUbc7Lysine residuesLiving cellsChain assemblyUbiquitinCysteineEnzymeSide chainsUfd4Cue1
1998
A Deubiquitinating Enzyme That Disassembles Free Polyubiquitin Chains Is Required for Development but Not Growth in Dictyostelium *
Lindsey D, Amerik A, Deery W, Bishop J, Hochstrasser M, Gomer R. A Deubiquitinating Enzyme That Disassembles Free Polyubiquitin Chains Is Required for Development but Not Growth in Dictyostelium *. Journal Of Biological Chemistry 1998, 273: 29178-29187. PMID: 9786928, DOI: 10.1074/jbc.273.44.29178.Peer-Reviewed Original ResearchConceptsUbiquitin polymersPolyubiquitin chainsUbiquitin chainsDeubiquitinating enzymeCross-species complementationFree ubiquitin chainsSpecific developmental transitionsWild-type cellsFree polyubiquitin chainsNormal protein profilesDictyostelium developmentFunctional homologSequence similarityCAMP receptorNew proteinsProtein degradationAdhesion proteinsWild typeDevelopmental transitionsSpecific proteinsExogenous cAMPCell differentiationProtein profilesSpecificity assaysCell adhesion
1997
In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome
Amerik A, Swaminathan S, Krantz B, Wilkinson K, Hochstrasser M. In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome. The EMBO Journal 1997, 16: 4826-4838. PMID: 9305625, PMCID: PMC1170118, DOI: 10.1093/emboj/16.16.4826.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCarbon-Nitrogen LyasesEndopeptidasesFungal ProteinsGene Expression Regulation, FungalGenes, FungalHumansImmunoblottingLyasesMolecular Sequence DataMutagenesis, Site-DirectedPeptide HydrolasesPhenotypeProteasome Endopeptidase ComplexProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSubstrate SpecificityUbiquitinsConceptsUnanchored ubiquitin chainsUbiquitin chainsProtein degradationFree ubiquitin chainsUbiquitin-dependent proteolysisWild-type cellsActive site mutantsFree polyubiquitin chainsEukaryotic proteinsFunctional homologComplementation analysisPolyubiquitin chainsSteady-state levelsDeubiquitinating enzymeUbp14Site mutantsIsopeptidase TCellular proteasesYeast cellsProteasomeInhibition of degradationStriking accumulationProteolysisProteinCells