The Unfolded Protein Response Triggers Site-Specific Regulatory Ubiquitylation of 40S Ribosomal Proteins
Higgins R, Gendron JM, Rising L, Mak R, Webb K, Kaiser SE, Zuzow N, Riviere P, Yang B, Fenech E, Tang X, Lindsay SA, Christianson JC, Hampton RY, Wasserman SA, Bennett EJ. The Unfolded Protein Response Triggers Site-Specific Regulatory Ubiquitylation of 40S Ribosomal Proteins. Molecular Cell 2015, 59: 35-49. PMID: 26051182, PMCID: PMC4491043, DOI: 10.1016/j.molcel.2015.04.026.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineCell SurvivalDrosophilaEIF-2 KinaseEndoplasmic ReticulumEndoplasmic Reticulum StressEukaryotic Initiation Factor-2Gene Expression RegulationHumansMolecular Sequence DataPhosphorylationProtein BiosynthesisRibosome Subunits, Small, EukaryoticSaccharomyces cerevisiaeUbiquitinationUnfolded Protein ResponseConceptsUnfolded protein responseRegulatory ubiquitylationRibosomal proteinsUPR activationEukaryotic translational controlUbiquitin-dependent regulationER-resident proteinsChronic UPR activationTranslational reprogrammingER homeostasisTranslational controlCytoplasmic ribosomesProtein foldingTranslation inhibitionProtein responseUbiquitylationPERK signalingUbiquitin proteomicsOptimal cell survivalCell survivalProtein synthesisProteinDegradation capacityReprogrammingActivation