2022
Elements of the ERAD ubiquitin ligase Doa10 regulating sequential poly-ubiquitylation of its targets
Mehrtash A, Hochstrasser M. Elements of the ERAD ubiquitin ligase Doa10 regulating sequential poly-ubiquitylation of its targets. IScience 2022, 25: 105351. PMID: 36325070, PMCID: PMC9619350, DOI: 10.1016/j.isci.2022.105351.Peer-Reviewed Original ResearchC-terminal elementsUbiquitin ligase Doa10RING-CH domainDoa10 substratesSubstrate ubiquitylationRetrotranslocation channelSingle ubiquitinIntragenic suppressionCofactor-binding regionPolyubiquitin chainsDoa10E3 ubiquitinER proteinsTruncation analysisStructural predictionsStructure predictionUBC6Ubc7UbiquitylationDirect roleMechanistic insightsE2 bindsUbiquitinBindsERAD
2013
Chapter 462 The Doa4 Deubiquitylating Enzyme (Saccharomyces cerevisiae)
Amerik A, Hochstrasser M. Chapter 462 The Doa4 Deubiquitylating Enzyme (Saccharomyces cerevisiae). 2013, 2049-2052. DOI: 10.1016/b978-0-12-382219-2.00461-0.Peer-Reviewed Original ResearchChapter 528 Ulp2 SUMO Protease
Gillies J, Su D, Hochstrasser M. Chapter 528 Ulp2 SUMO Protease. 2013, 2362-2365. DOI: 10.1016/b978-0-12-382219-2.00526-3.Peer-Reviewed Original Research
2010
Chapter 161 The Ubiquitin–Proteasome System
Hochstrasser M. Chapter 161 The Ubiquitin–Proteasome System. 2010, 1293-1296. DOI: 10.1016/b978-0-12-374145-5.00161-3.Peer-Reviewed Original ResearchUbiquitin-proteasome systemC-terminusMultimeric protein complexesMultiple ubiquitin moietiesFree ubiquitin poolMost DUBsUbiquitin additionUbiquitin removalUbiquitylated proteinsIndividual physiological functionsProtein complexesE1 enzymeUbiquitin moietiesUbiquitin genesUbiquitin ligationIntrinsic subunitsUbiquitin sequenceAcceptor proteinsIsopeptide bondsUbiquitin poolsUbiquitinPhysiological functionsPrecursor formDUBsIntracellular nucleophiles
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
2007
Biochemical Functions of Ubiquitin and Ubiquitin‐like Protein Conjugation
Hochstrasser M. Biochemical Functions of Ubiquitin and Ubiquitin‐like Protein Conjugation. 2007, 249-278. DOI: 10.1002/9783527619320.ch11a.Peer-Reviewed Original ResearchSUMO-binding motifMembrane protein traffickingUbiquitin receptorsMVB pathwayUbl conjugationGeneral biochemical functionsBiochemical functionsPositive regulationNegative regulationProtein traffickingProteasome pathwayUbiquitin-like protein conjugationProtein ubiquitinRNA virus buddingCross regulationChange interactionsModification cyclesVirus buddingUbiquitinSulfurtransferasesProteasomeMotifSUMOylationRegulationPathway
2005
Biochemical Functions of Ubiquitin and Ubiquitin‐like Protein Conjugation
Hochstrasser M. Biochemical Functions of Ubiquitin and Ubiquitin‐like Protein Conjugation. 2005, 249-278. DOI: 10.1002/9783527620210.ch11.Peer-Reviewed Original ResearchSUMO-binding motifMembrane protein traffickingUbiquitin receptorsMVB pathwayUbl conjugationGeneral biochemical functionsBiochemical functionsPositive regulationNegative regulationProtein traffickingProteasome pathwayUbiquitin-like protein conjugationProtein ubiquitinRNA virus buddingCross regulationChange interactionsModification cyclesVirus buddingUbiquitinSulfurtransferasesProteasomeMotifSUMOylationRegulationPathway
2003
Chapter 181 The Ubiquitin-Proteasome System
Hochstrasser M. Chapter 181 The Ubiquitin-Proteasome System. 2003, 347-350. DOI: 10.1016/b978-012124546-7/50542-8.Peer-Reviewed Original ResearchUbiquitin-proteasome systemProtein ubiquitinationMembrane proteinsFunction of ubiquitinUbiquitin-dependent proteolysisCellular regulatory mechanismsCell cycle controlSignal transduction pathwaysNegative cell cycle regulatorsCell cycle regulatorsKey regulatory pathwaysSubstrate proteinsMitotic exitProtein phosphorylationTransduction pathwaysRegulatory pathwaysC-terminusCycle controlRegulatory mechanismsIntracellular proteinsCell cycleUbiquitinationTimed degradationProteinUbiquitin
2000
Evolution and function of ubiquitin-like protein-conjugation systems
Hochstrasser M. Evolution and function of ubiquitin-like protein-conjugation systems. Nature Cell Biology 2000, 2: e153-e157. PMID: 10934491, DOI: 10.1038/35019643.Peer-Reviewed Original ResearchA viable ubiquitin‐activating enzyme mutant for evaluating ubiquitin system function in Saccharomyces cerevisiae
Swanson R, Hochstrasser M. A viable ubiquitin‐activating enzyme mutant for evaluating ubiquitin system function in Saccharomyces cerevisiae. FEBS Letters 2000, 477: 193-198. PMID: 10908719, DOI: 10.1016/s0014-5793(00)01802-0.Peer-Reviewed Original ResearchConceptsUbiquitin system functionActivation of ubiquitinUbiquitin-activating enzymeProteasome-independent degradationUbiquitin systemCellular processesPathway substrateMammalian cellsHypomorphic alleleProtein modificationEnzyme mutantsMutant allelesMembrane receptorsMutantsUbiquitinComparable mutantsSaccharomycesCell functionAllelesProteasomeYeastProteinEnzymeDegradationE1
1999
The Doa4 Deubiquitinating Enzyme Is Required for Ubiquitin Homeostasis in Yeast
Swaminathan S, Amerik A, Hochstrasser M. The Doa4 Deubiquitinating Enzyme Is Required for Ubiquitin Homeostasis in Yeast. Molecular Biology Of The Cell 1999, 10: 2583-2594. PMID: 10436014, PMCID: PMC25490, DOI: 10.1091/mbc.10.8.2583.Peer-Reviewed Original ResearchMeSH KeywordsCarrier ProteinsCytoskeletal ProteinsEndopeptidasesEndosomal Sorting Complexes Required for TransportFungal ProteinsHomeostasisMutationPeptide HydrolasesProteasome Endopeptidase ComplexSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin ThiolesteraseUbiquitinsVacuolesVesicular Transport ProteinsConceptsDeubiquitinating enzymeAttachment of ubiquitinUbiquitin-dependent proteolysisYeast Saccharomyces cerevisiaeWild-type cellsCell surface proteinsAdditional ubiquitinVacuolar proteolysisUbiquitinated substratesUbiquitin homeostasisCellular proteinsMembrane proteinsUbiquitinated intermediatesSaccharomyces cerevisiaeGenetic dataDoa4Loss of viabilityUbiquitin depletionUbiquitinProteolytic intermediatesProteasomeSurface proteinsUbiquitin degradationEventual degradationProteinA new protease required for cell-cycle progression in yeast
Li S, Hochstrasser M. A new protease required for cell-cycle progression in yeast. Nature 1999, 398: 246-251. PMID: 10094048, DOI: 10.1038/18457.Peer-Reviewed Original ResearchMeSH KeywordsCarrier ProteinsCell Cycle ProteinsCloning, MolecularCysteine EndopeptidasesEscherichia coliFungal ProteinsG2 PhaseHumansMitosisMolecular Sequence DataMutagenesisRecombinant Fusion ProteinsRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSmall Ubiquitin-Related Modifier ProteinsSubstrate SpecificitySUMO-1 ProteinUbiquitinsConceptsSUMO-1Cell cycleUbl-specific proteasesUbiquitin-like proteinCell cycle progressionG2/M phaseProtein functionSmt3Cellular proteinsDeubiquitinating enzymeUlp1Distant similarityUbiquitinHuman pathogensM phaseProteinEssential roleNew proteaseProteaseViral proteaseProtein conjugationEukaryotesMutantsUBLYeast
1998
The Deubiquitinating Enzymes
Wilkinson K, Hochstrasser M. The Deubiquitinating Enzymes. 1998, 99-125. DOI: 10.1007/978-1-4899-1922-9_4.Peer-Reviewed Original ResearchPolyubiquitin chainsTypes of ubiquitinationReceptor-mediated signal transductionCell cycle progressionModification of proteinsOrganelle biogenesisUbiquitin polypeptidesChromosome structureUbiquitin moleculesCellular processesProtein localizationSignal transductionDeubiquitinating enzymeIsopeptide linkageLysine 48Lysine 6C-terminusGene expressionIsopeptide bondsStress responseUbiquitinProteinProtein metabolismViral pathogenesisBiogenesis
1997
SUMO-1: Ubiquitin gains weight
Johnson P, Hochstrasser M. SUMO-1: Ubiquitin gains weight. Trends In Cell Biology 1997, 7: 408-413. PMID: 17708991, DOI: 10.1016/s0962-8924(97)01132-x.Peer-Reviewed Original ResearchNuclear pore complexUbiquitin-like proteinNucleocytoplasmic traffickingPore complexUbiquitin systemPolypeptide functionsProtein crucialSUMO-1Cell biologyDistant similaritySpecific proteinsMechanistic questionsProteinSubstrate degradationProteasomeRecent findingsUbiquitinTraffickingBiologyRoleModificationCrucialComplexesSimilarity
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
1994
Degradation of the yeast MATα2 transcriptional regulator is mediated by the proteasome
Richter-Ruoff B, Wolf D, Hochstrasser M. Degradation of the yeast MATα2 transcriptional regulator is mediated by the proteasome. FEBS Letters 1994, 354: 50-52. PMID: 7957900, DOI: 10.1016/0014-5793(94)01085-4.Peer-Reviewed Original ResearchConceptsSpecific regulatory proteinsMulti-subunit proteaseSelective protein turnoverCell cycle progressionPolypeptide ubiquitinTranscriptional regulatorsCellular proteinsRegulatory proteinsCellular phenomenaCovalent ligationCycle progressionIntracellular proteolysisProtein turnoverProteasomeCell growthRapid degradationMajor mechanismProteinRepressorUbiquitinVivoDegradationRegulatorProteolysisProtease
1993
The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene
Papa F, Hochstrasser M. The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene. Nature 1993, 366: 313-319. PMID: 8247125, DOI: 10.1038/366313a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceEndopeptidasesEndosomal Sorting Complexes Required for TransportFungal ProteinsGenes, FungalHumansMiceMice, NudeMolecular Sequence DataMutationOncogene ProteinsOncogene Proteins, FusionOncogenesOpen Reading FramesPhenotypeProto-Oncogene ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidUbiquitin ThiolesteraseUbiquitinsMultiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor
Chen P, Johnson P, Sommer T, Jentsch S, Hochstrasser M. Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor. Cell 1993, 74: 357-369. PMID: 8393731, DOI: 10.1016/0092-8674(93)90426-q.Peer-Reviewed Original ResearchConceptsUbiquitin-conjugatingAttachment of ubiquitinUbiquitin-conjugating enzymeUBC proteinUbiquitination complexMolecular functionsTranscriptional regulatorsUbiquitination pathwayCellular processesSubstrate specificityDegradation signalPhysiological targetsSubstrate selectionCombinatorial mechanismsUnexpected overlapUBC6Intracellular degradationEnzymeProteinAlpha 2PathwayUbc7Deg1RepressorUbiquitin