2016
Human Atg8-cardiolipin interactions in mitophagy: Specific properties of LC3B, GABARAPL2 and GABARAP
Antón Z, Landajuela A, Hervás JH, Montes LR, Hernández-Tiedra S, Velasco G, Goñi FM, Alonso A. Human Atg8-cardiolipin interactions in mitophagy: Specific properties of LC3B, GABARAPL2 and GABARAP. Autophagy 2016, 12: 2386-2403. PMID: 27764541, PMCID: PMC5172498, DOI: 10.1080/15548627.2016.1240856.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceApoptosis Regulatory ProteinsAutophagyAutophagy-Related Protein 8 FamilyCardiolipinsCell Line, TumorCell MembraneDronabinolGlioblastomaHumansHydrophobic and Hydrophilic InteractionsMicrotubule-Associated ProteinsMitochondriaMitochondrial MembranesMitophagyPressureProtein BindingRotenoneSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidConceptsSelective mitochondrial autophagyOuter mitochondrial membraneHuman Atg8Quantitative biophysical techniquesHuman orthologAutophagosome formationMitochondrial autophagyMitochondrial membraneAutophagic processC-terminusGABARAPL2GABARAPPhospholipid cardiolipinBiophysical techniquesMitochondriaOrthologsMembrane fluidityCardiolipinLC3BMitophagyPositive cooperativitySpecific roleU87MG cellsAutophagyHydrophilic environmentLipid Geometry and Bilayer Curvature Modulate LC3/GABARAP-Mediated Model Autophagosomal Elongation
Landajuela A, Hervás JH, Antón Z, Montes LR, Gil D, Valle M, Rodriguez JF, Goñi FM, Alonso A. Lipid Geometry and Bilayer Curvature Modulate LC3/GABARAP-Mediated Model Autophagosomal Elongation. Biophysical Journal 2016, 110: 411-422. PMID: 26789764, PMCID: PMC4724631, DOI: 10.1016/j.bpj.2015.11.3524.Peer-Reviewed Original ResearchConceptsMembrane fusionCryo-electron microscopy observationsFull membrane fusionNegative intrinsic curvature lipidsCurvature-inducing lipidsImportant catabolic pathwayMultiple fusion eventsAtg8 homologsMembrane tetheringGABARAP proteinsLytic compartmentAP biogenesisGATE-16Fusion eventsIntervesicular mixingCatabolic pathwayMembrane expansionVesicle aggregationMolecular mechanismsLipid geometryVesicle diameterHuman diseasesIntervesicular lipid mixingImportant regulatorLarge vesicles
2014
Lipid-Dependent Bimodal MCL1 Membrane Activity
Landeta O, Valero J, Flores-Romero H, Bustillo-Zabalbeitia I, Landajuela A, Garcia-Porras M, Terrones O, Basañez G. Lipid-Dependent Bimodal MCL1 Membrane Activity. ACS Chemical Biology 2014, 9: 2852-2863. PMID: 25314294, DOI: 10.1021/cb500592e.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBcl-2-Associated X ProteinBH3 Interacting Domain Death Agonist ProteinCardiolipinsCholesterolFibroblastsGene ExpressionHeLa CellsHumansLiposomesMembrane LipidsMembrane Potential, MitochondrialMiceMitochondriaModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMyeloid Cell Leukemia Sequence 1 ProteinPhosphatidylinositolsProtein Structure, TertiaryProto-Oncogene Proteins c-bcl-2Recombinant ProteinsSequence AlignmentConceptsPore-forming activityProtein functionConformational changesMitochondrial membrane lipidsLipid membrane environmentSite-directed mutagenesisProfound conformational changesNovel mechanistic insightsMembrane integrationCanonical BH3Homology regionMembrane environmentMembrane permeabilizationMitochondrial lipidsMinimal domainMembrane lipidsMitochondrial levelGroove interactionsProapoptotic partnersMcl1 activityMechanistic insightsMembrane activityModel membranesFluorescence spectroscopic analysisPermeabilization