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
2023
Proteasomes: Isolation and Activity Assays
Li Y, Tomko R, Hochstrasser M. Proteasomes: Isolation and Activity Assays. Current Protocols 2023, 3: e717. PMID: 37026813, PMCID: PMC10337785, DOI: 10.1002/cpz1.717.Peer-Reviewed Original ResearchConceptsRegulatory particleOne-step purification schemeCore particlesMultisubunit protease complexUbiquitin-proteasome systemUbiquitin polypeptidesUnneeded proteinsYeast SaccharomycesProtein substratesProtease complexProteasomeGel filtration stepPurification schemeProteolytic activityEukaryotesSaccharomycesPolypeptideProteinSubstrateAssaysComplexes
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
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
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
1999
Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N‐terminal acetylation and promote particle assembly
Arendt C, Hochstrasser M. Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N‐terminal acetylation and promote particle assembly. The EMBO Journal 1999, 18: 3575-3585. PMID: 10393174, PMCID: PMC1171436, DOI: 10.1093/emboj/18.13.3575.Peer-Reviewed Original ResearchMeSH KeywordsAcetylationAmino Acid SequenceArylamine N-AcetyltransferaseBinding SitesCatalysisCatalytic DomainCell DivisionCysteine EndopeptidasesEndopeptidasesFungal ProteinsIsoenzymesMolecular Sequence DataMultienzyme ComplexesPeptide FragmentsPhenotypeProteasome Endopeptidase ComplexSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence DeletionThreonineConceptsProteasome assemblyFirst biochemical evidenceN-terminal acetylationUbiquitin-proteasome systemProteolytic active sitesBarrel-shaped structureCatalytic threonine residueYeast 20S proteasomeThreonine residuesHeptameric ringsProteasome biogenesisEnvironmental stressNovel functionDistinct functionsLarge proteaseDifferent subunitsParticle assemblyAlpha-amino groupSpecific peptidase activityProteasomeCatalytic mechanismSite inactivationPeptidase activityCritical functionsSubunits