2024
Limiting 20S proteasome assembly leads to unbalanced nucleo-cytoplasmic distribution of 26S/30S proteasomes and chronic proteotoxicity
Ruiz-Romero G, Berdún M, Hochstrasser M, Salas-Pino S, Daga R. Limiting 20S proteasome assembly leads to unbalanced nucleo-cytoplasmic distribution of 26S/30S proteasomes and chronic proteotoxicity. IScience 2024, 27: 111095. PMID: 39473973, PMCID: PMC11513537, DOI: 10.1016/j.isci.2024.111095.Peer-Reviewed Original ResearchProteasome assemblyDegradation of cell cycle proteinsNucleo-cytoplasmic distributionCell cycle proteinsHeat shock responseCytoplasmic proteostasisFission yeastMitotic substratesProteasome regulationCytoplasmic aggregatesUnfolded proteinsProteasome activityProteasomeConstitutive activationFunctional relevanceShock responseUmp1Cell proliferationProteinCellsCompartmentalizationAssemblyProteostasisYeastChaperone
2017
Pba3‐Pba4 Plays a Role in Preventing Non‐Productive Interactions Among the α Subunits of the Proteasome
Panfair D, Ramamurthy A, Hochstrasser M, Kusmierczyk A. Pba3‐Pba4 Plays a Role in Preventing Non‐Productive Interactions Among the α Subunits of the Proteasome. The FASEB Journal 2017, 31 DOI: 10.1096/fasebj.31.1_supplement.917.1.Peer-Reviewed Original ResearchProteasome assemblyDegradation of ubiquitin-tagged proteinsMultisubunit protease complexUbiquitin-tagged proteinsNon-productive interactionsEarly eventMolecular weight complexesAssembly chaperonesTagged proteinsSubunit additionRecombinant expressionProtease complexEscherichia coliDead-end speciesProteasomeWeight complexesSubunitRing complexCoexpressionIn vivoAssemblyCrosslinking strategyChaperoneA ringSpecies