2024
Yeast 26S proteasome nuclear import is coupled to nucleus-specific degradation of the karyopherin adaptor protein Sts1
Breckel C, Johnson Z, Hickey C, Hochstrasser M. Yeast 26S proteasome nuclear import is coupled to nucleus-specific degradation of the karyopherin adaptor protein Sts1. Scientific Reports 2024, 14: 2048. PMID: 38267508, PMCID: PMC10808114, DOI: 10.1038/s41598-024-52352-5.Peer-Reviewed Original ResearchConceptsProteasome storage granulesNuclear importUbiquitin-independent proteasomal degradationProteasome degradation in vitroYeast Saccharomyces cerevisiaeProlonged glucose starvationNuclear import factorsUbiquitin-proteasome systemProteasome interactionGlucose starvationKaryopherin proteinsProteasomal degradationNuclear transportCellular homeostasisDegradation in vivoSTS1KaryopherinProtein degradationProteasomeDegradation in vitroGlucose refeedingStorage granulesProteinEukaryotesRanGTP
2020
The Relationship between ER Stress and Protein Quality Control at the Translocon
Broshar C, Buchanan B, Mehrtash A, Runnebohm A, Snow B, Scanameo L, Hochstrasser M, Rubenstein E. The Relationship between ER Stress and Protein Quality Control at the Translocon. The FASEB Journal 2020, 34: 1-1. DOI: 10.1096/fasebj.2020.34.s1.00497.Peer-Reviewed Original ResearchProtein quality controlUbiquitin-proteasome systemER stressUbiquitin ligaseDegradation signalProtein quality control mechanismsHrd1 ubiquitin ligaseTranslocon-associated proteinLipid homeostasisStress-sensing mechanismsStress-responsive mechanismsQuality control mechanismsDegradation of proteinsERAD pathwayModel organismsEndoplasmic reticulum stressProtein misfoldingAberrant proteinsERADImpairs degradationProtein degradationProteins misfoldHeat shockEndoplasmic reticulumProtein
2008
Ubiquitin and Ubiquitin‐like Protein Conjugation
Hochstrasser M. Ubiquitin and Ubiquitin‐like Protein Conjugation. 2008, 249-278. DOI: 10.1002/9783527610754.mr02.Peer-Reviewed Original ResearchEukaryotic cell regulationR. John MayerUbiquitin-like proteinConjugation systemAaron CiechanoverEvolutionary originMartin RechsteinerMost ubiquitinUbl systemsProtein modifiersProtein modificationProtein degradationBiological processesUbiquitinCell regulationMacromolecular interactionsRelated enzymesEnormous arrayProteinDistinct mechanismsConjugated proteinsFunctional featuresRapid degradationPervasive roleJohn MayerAn 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
1996
UBIQUITIN-DEPENDENT PROTEIN DEGRADATION
Hochstrasser M. UBIQUITIN-DEPENDENT PROTEIN DEGRADATION. Annual Review Of Genetics 1996, 30: 405-439. PMID: 8982460, DOI: 10.1146/annurev.genet.30.1.405.Peer-Reviewed Original ResearchConceptsRegulatory mechanismsUbiquitin-dependent protein degradationLarge enzyme familyAttachment of ubiquitinCellular regulatory mechanismsSignal transduction pathwaysHigh substrate specificityReceptor-mediated endocytosisPolypeptide ubiquitinProtein ubiquitinationUbiquitin systemTransduction pathwaysEnzyme familyUbiquitinated proteinsSubstrate specificityProtein modificationProtein degradationCell cycleProteasomeUbiquitinationKey transitionsUbiquitinShort peptidesProteinDeubiquitination
1995
Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
Hochstrasser M. Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Current Opinion In Cell Biology 1995, 7: 215-223. PMID: 7612274, DOI: 10.1016/0955-0674(95)80031-x.Peer-Reviewed Original ResearchConceptsCellular regulatory mechanismsIntracellular protein degradationCell cycle progressionProtein ubiquitinationUbiquitin systemProtein degradationRegulatory mechanismsCycle progressionSpecific proteinsForeign proteinsLarge familyCell proliferationProteasomeRapid degradationProteinClass I MHC moleculesUbiquitinationDeubiquitinationUbiquitinI MHC moleculesProteolysisEnzymeKey stepDegradationRegulation
1992
Ubiquitin and intracellular protein degradation
Hochstrasser M. Ubiquitin and intracellular protein degradation. Current Opinion In Cell Biology 1992, 4: 1024-1031. PMID: 1336669, DOI: 10.1016/0955-0674(92)90135-y.Peer-Reviewed Original ResearchConceptsEukaryotic cell regulationConjugation of ubiquitinUbiquitin systemProteolytic targetingProtein degradationIntracellular proteinsProtein turnoverCell regulationDiverse arrayUbiquitinCentral roleProteinEukaryotesMajor routeUbiquitinationProteaseEnzymeDegradationPathwayRegulationRecent workTargetingTurnoverPeptides
1991
Functions of Intracellular Protein Degradation in Yeast
Hochstrasser M. Functions of Intracellular Protein Degradation in Yeast. Genetic Engineering: Principles And Methods 1991, 13: 307-329. PMID: 1369338, DOI: 10.1007/978-1-4615-3760-1_14.Peer-Reviewed Original Research