2023
Sis2 regulates yeast replicative lifespan in a dose-dependent manner
Ölmez T, Moreno D, Liu P, Johnson Z, McGinnis M, Tu B, Hochstrasser M, Acar M. Sis2 regulates yeast replicative lifespan in a dose-dependent manner. Nature Communications 2023, 14: 7719. PMID: 38012152, PMCID: PMC10682402, DOI: 10.1038/s41467-023-43233-y.Peer-Reviewed Original ResearchConceptsYeast replicative lifespanReplicative lifespanRNA-seq experimentsCoenzyme A biosynthesis pathwayYeast lifespanYeast strainsStrain librariesLifespan regulationRNA-seqGene networksDose-dependent mannerLifespan extensionTranscriptional increaseYeastLifespan measurementsWild-typeGenesMachinery componentsStrainMicrofluidic platformApplications of microfluidic platformsLifespanDeletionCoenzymePathwayEctopic RING activity at the ER membrane differentially impacts ERAD protein quality control pathways
Mehrtash A, Hochstrasser M. Ectopic RING activity at the ER membrane differentially impacts ERAD protein quality control pathways. Journal Of Biological Chemistry 2023, 299: 102927. PMID: 36682496, PMCID: PMC9950527, DOI: 10.1016/j.jbc.2023.102927.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulum-associated degradationProtein quality control pathwaysQuality control pathwaysER membraneE3 complexControl pathwaysRING-type E3 ubiquitin ligasesE3 ubiquitin ligasesDominant negative mutantDoa10 substratesMisfolded proteinsUbiquitin ligasesERAD factorsMammalian cellsRING domainUBC6Substrate turnoverLuminal substratesDoa10OverexpressionPathway defectsYeastPathwayRing activityMembrane
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
1999
Interaction of the Doa4 Deubiquitinating Enzyme with the Yeast 26S Proteasome
Papa F, Amerik A, Hochstrasser M. Interaction of the Doa4 Deubiquitinating Enzyme with the Yeast 26S Proteasome. Molecular Biology Of The Cell 1999, 10: 741-756. PMID: 10069815, PMCID: PMC25199, DOI: 10.1091/mbc.10.3.741.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCysteine EndopeptidasesEndopeptidasesEndosomal Sorting Complexes Required for TransportFungal ProteinsMolecular Sequence DataMultienzyme ComplexesProteasome Endopeptidase ComplexRecombinant ProteinsSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidStructure-Activity RelationshipUbiquitin ThiolesteraseYeastsConceptsRemoval of ubiquitinUbiquitin-proteasome pathwayYeast 26S ProteasomeProteasome bindingGenetic interactionsProteasome mutationsDoa4Protein substratesCatalytic domainDeubiquitinating enzymeUbp5Physical associationProteolytic intermediatesProteasomeN-terminalFunctional interactionEnzymeRecombination methodRapid degradationMutationsPurification procedurePathwaySubstrate breakdownCopurifiesSaccharomyces
1998
Degradation Signal Masking by Heterodimerization of MATα2 and MATa1 Blocks Their Mutual Destruction by the Ubiquitin-Proteasome Pathway
Johnson P, Swanson R, Rakhilina L, Hochstrasser M. Degradation Signal Masking by Heterodimerization of MATα2 and MATa1 Blocks Their Mutual Destruction by the Ubiquitin-Proteasome Pathway. Cell 1998, 94: 217-227. PMID: 9695950, DOI: 10.1016/s0092-8674(00)81421-x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCysteine EndopeptidasesDimerizationDiploidyFungal ProteinsHaploidyIntramolecular TransferasesLipoproteinsMating FactorMolecular Sequence DataMultienzyme ComplexesMutationPeptidesPheromonesProteasome Endopeptidase ComplexProtein Structure, SecondarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinsConceptsUbiquitin-proteasome pathwayDegradation signalCoiled-coil interactionsAlpha haploid cellsRegulated turnoverMultiprotein complexesHaploid cellsPathway substrateTranscription factorsExtensive mutagenesisProteolytic signalMolecular mechanismsCell typesHeterodimerizationSuch regulationCritical determinantPathwayAlpha2MATa1MATα2Signal maskingRepressorHaploidsSaccharomycesMutagenesisUbiquitin-Dependent Degradation of Transcription Regulators
Hochstrasser M, Kornitzer D. Ubiquitin-Dependent Degradation of Transcription Regulators. 1998, 279-302. DOI: 10.1007/978-1-4899-1922-9_9.Peer-Reviewed Original ResearchTranscription factorsTranscription regulatorsBacterial transcription factorsYeast transcription factorUbiquitin-dependent degradationUbiquitin-proteasome pathwayActivity of proteinsTranscription factor c-FosMain regulatory proteinTranscription initiationCellular proteinsRegulatory proteinsC-MycProteinMost cellsRegulatorIntracellular levelsExamples of degradationC-fosRapid modulationPathwayNumerous levelsEukaryotesMATα2Σ32
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
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
1990
In vivo degradation of a transcriptional regulator: The yeast α2 repressor
Hochstrasser M, Varshavsky A. In vivo degradation of a transcriptional regulator: The yeast α2 repressor. Cell 1990, 61: 697-708. PMID: 2111732, DOI: 10.1016/0092-8674(90)90481-s.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBeta-GalactosidaseFungal ProteinsGene Expression Regulation, FungalHalf-LifeMacromolecular SubstancesMolecular Sequence DataMutationProtein EngineeringProtein Processing, Post-TranslationalRecombinant Fusion ProteinsRepressor ProteinsSaccharomyces cerevisiaeTranscription FactorsConceptsYeast S. cerevisiaeTranscriptional regulatorsHeteromeric proteinsAlpha 2S. cerevisiaeDegradation signalRegulatory proteinsOligomeric proteinsSame proteinStructural domainsProteinMultiple functionsSubunitsRepressorDistinct mechanismsVivo concentrationsAdditional defectsCerevisiaeMutantsNovel typeDegradationRegulatorPathwayMetabolic instabilityVivo degradation