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
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
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 maskingRepressorHaploidsSaccharomycesMutagenesis
1993
Multiple 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
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