2022
Polybasic Patches in Both C2 Domains of Synaptotagmin-1 Are Required for Evoked Neurotransmitter Release
Wu Z, Ma L, Courtney NA, Zhu J, Landajuela A, Zhang Y, Chapman ER, Karatekin E. Polybasic Patches in Both C2 Domains of Synaptotagmin-1 Are Required for Evoked Neurotransmitter Release. Journal Of Neuroscience 2022, 42: 5816-5829. PMID: 35701163, PMCID: PMC9337609, DOI: 10.1523/jneurosci.1385-21.2022.Peer-Reviewed Original ResearchConceptsSynaptotagmin-1C2 domainSynchronous neurotransmitter releaseSNARE proteinsPlasma membraneCalcium sensorSingle-pass transmembrane domainOptical tweezers measurementsSynaptic vesiclesAcidic lipidsNeurotransmitter releaseBind calciumCharge neutralization mutationsEvoked Neurotransmitter ReleaseReleasable vesicle poolSyt1 functionSNARE complexPolybasic regionOverall affinityTransmembrane domainMembrane bindingSingle-molecule experimentsC2A domainSynchronous releaseVesicle pool
2015
Minimalist Model Systems Reveal Similarities and Differences between Membrane Interaction Modes of MCL1 and BAK*
Landeta O, Landajuela A, Garcia-Saez A, Basañez G. Minimalist Model Systems Reveal Similarities and Differences between Membrane Interaction Modes of MCL1 and BAK*. Journal Of Biological Chemistry 2015, 290: 17004-17019. PMID: 25987560, PMCID: PMC4505444, DOI: 10.1074/jbc.m114.602193.Peer-Reviewed Original ResearchConceptsBCL2 family proteinsFamily proteinsStructural foldMembrane environmentStable heterodimeric complexMembrane association modesFluorescence cross-correlation spectroscopyBCL2 family membersMembrane interaction modesCross-correlation spectroscopyCell fateMembrane associationHeterodimeric complexBCL2 familyMitochondrial membraneCellular factorsFluorescence-based techniquesMode of actionApoptosis-related factorsBakKey modulatorFRET measurementsMCL1ProteinCardiolipin content
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
2013
Proapoptotic Bax and Bak Proteins Form Stable Protein-permeable Pores of Tunable Size
Bleicken S, Landeta O, Landajuela A, Basañez G, García-Sáez A. Proapoptotic Bax and Bak Proteins Form Stable Protein-permeable Pores of Tunable Size. Journal Of Biological Chemistry 2013, 288: 33241-33252. PMID: 24100034, PMCID: PMC3829170, DOI: 10.1074/jbc.m113.512087.Peer-Reviewed Original ResearchConceptsMitochondrial outer membraneApoptotic poreOuter membraneMitochondrial apoptotic factorsSingle vesicle levelActivity of BaxProapoptotic protein BaxProteinaceous channelsVesicle levelMembrane permeabilizationBak proteinForm poresProtein BaxProapoptotic BaxCardiolipin concentrationCytochrome cApoptotic factorsBaxBakPermeabilizationProteinSimilar mechanismMembraneMembrane poresProtein concentration