2021
Atg39 selectively captures inner nuclear membrane into lumenal vesicles for delivery to the autophagosome
Chandra S, Mannino PJ, Thaller DJ, Ader NR, King MC, Melia TJ, Lusk CP. Atg39 selectively captures inner nuclear membrane into lumenal vesicles for delivery to the autophagosome. Journal Of Cell Biology 2021, 220: e202103030. PMID: 34714326, PMCID: PMC8575018, DOI: 10.1083/jcb.202103030.Peer-Reviewed Original ResearchMeSH KeywordsAutophagosomesAutophagyAutophagy-Related ProteinsCytoplasmic VesiclesGreen Fluorescent ProteinsNuclear EnvelopeProtein DomainsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipTime FactorsVacuolesVesicular Transport ProteinsConceptsInner nuclear membraneNuclear envelope lumenOuter nuclear membraneNuclear membraneSplit-GFP reporterNuclear envelope localizationINM proteinsAutophagy apparatusEnvelope localizationLumenal vesiclesLumenal domainCargo adaptorsAtg39Sequence elementsCorrelative lightVesiclesAutophagosomesMembraneNucleophagyAdaptorReporterProteinOverexpressionMotif
2018
Delipidation of mammalian Atg8-family proteins by each of the four ATG4 proteases
Kauffman KJ, Yu S, Jin J, Mugo B, Nguyen N, O'Brien A, Nag S, Lystad AH, Melia TJ. Delipidation of mammalian Atg8-family proteins by each of the four ATG4 proteases. Autophagy 2018, 14: 992-1010. PMID: 29458288, PMCID: PMC6103404, DOI: 10.1080/15548627.2018.1437341.Peer-Reviewed Original ResearchConceptsAtg8-family proteinsAtg4 proteasesATG8 proteinsMammalian Atg8 proteinsMacroautophagy/autophagySimilar enzymatic activityProteolytic processing eventsLIR motifATG4 familyProcessing eventsPhysical anchoringProteinEnzymatic activityProteaseSoluble substratesATG4BTerminal glycinePhagophoreHomologLipidsDelipidationAutophagosomesAutophagyMotifSubstrate
2014
Lipidation of the LC3/GABARAP family of autophagy proteins relies on a membrane-curvature-sensing domain in Atg3
Nath S, Dancourt J, Shteyn V, Puente G, Fong WM, Nag S, Bewersdorf J, Yamamoto A, Antonny B, Melia TJ. Lipidation of the LC3/GABARAP family of autophagy proteins relies on a membrane-curvature-sensing domain in Atg3. Nature Cell Biology 2014, 16: 415-424. PMID: 24747438, PMCID: PMC4111135, DOI: 10.1038/ncb2940.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid MotifsAnimalsApoptosis Regulatory ProteinsAutophagy-Related Protein 7Autophagy-Related Protein 8 FamilyAutophagy-Related ProteinsCell MembraneCytoskeletal ProteinsHeLa CellsHumansHydrophobic and Hydrophilic InteractionsLiposomesMembrane ProteinsMiceMice, KnockoutMicrofilament ProteinsMicrotubule-Associated ProteinsMutationPhosphatidylethanolaminesRatsSignal TransductionStress, PhysiologicalTransfectionUbiquitin-Activating EnzymesUbiquitin-Conjugating EnzymesConceptsLipid-packing defectsLC3/GABARAP familyLC3/GABARAP lipidationAmino-terminal amphipathic helixE2-like enzymeGABARAP familyAutophagic machineryIsolation membraneAmphipathic helixIntracellular membranesAutophagy proteinsRescue experimentsATG3LipidationCurved rimProteinMotifPhysiologic roleMembranePhagophoreAutophagosomesMachineryHelixEnzyme