2000
The Doa4 Deubiquitinating Enzyme Is Functionally Linked to the Vacuolar Protein-sorting and Endocytic Pathways
Amerik A, Nowak J, Swaminathan S, Hochstrasser M. The Doa4 Deubiquitinating Enzyme Is Functionally Linked to the Vacuolar Protein-sorting and Endocytic Pathways. Molecular Biology Of The Cell 2000, 11: 3365-3380. PMID: 11029042, PMCID: PMC14998, DOI: 10.1091/mbc.11.10.3365.Peer-Reviewed Original ResearchMeSH KeywordsAdenocarcinomaAmino Acid SequenceBreast NeoplasmsCysteine EndopeptidasesEndocytosisEndopeptidasesEndosomal Sorting Complexes Required for TransportFemaleFungal ProteinsGenotypeHumansMolecular Sequence DataMultienzyme ComplexesMutagenesisProteasome Endopeptidase ComplexRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSequence Homology, Amino AcidSubstrate SpecificitySuppression, GeneticUbiquitin ThiolesteraseUbiquitinsVacuolesConceptsPrevacuolar compartmentDeubiquitinating enzymeVacuolar protein sorting (VPS) pathwayFluorescent proteinEndomembrane protein traffickingProtein sorting pathwaysUbiquitinated membrane proteinsVacuolar protein sortingClass E compartmentSpontaneous extragenic suppressorsGreen fluorescent proteinExtragenic suppressorsProtein sortingProtein traffickingProtein deubiquitinationUbiquitin recyclingPathway substrateE compartmentMembrane proteinsEndocytic pathwayUbiquitinated intermediatesDifferent genesMultivesicular bodiesNuclear distributionUnanticipated connectionsA 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
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