2018
Seeing the long tail: A novel green fluorescent protein, SiriusGFP, for ultra long timelapse imaging
Zhong S, Rivera-Molina F, Rivetta A, Toomre D, Santos-Sacchi J, Navaratnam D. Seeing the long tail: A novel green fluorescent protein, SiriusGFP, for ultra long timelapse imaging. Journal Of Neuroscience Methods 2018, 313: 68-76. PMID: 30578868, PMCID: PMC9431725, DOI: 10.1016/j.jneumeth.2018.12.008.Peer-Reviewed Original ResearchConceptsSuper-resolution structured illumination microscopyFluorescent proteinNovel green fluorescent proteinGreen fluorescent proteinMembrane proteinsPhotostable variantsCell biologyC-terminusStructured illumination microscopyEGFPProteinConfocal imagingSIM imagingCombination of novelIllumination microscopyKey mutationsKnown mutationsOmp25High intensity excitationMutationsLight intensityCo-operative effectSustained fluorescencePhotobleachingMisfolding
2017
Current carried by the Slc26 family member prestin does not flow through the transporter pathway
Bai JP, Moeini-Naghani I, Zhong S, Li FY, Bian S, Sigworth FJ, Santos-Sacchi J, Navaratnam D. Current carried by the Slc26 family member prestin does not flow through the transporter pathway. Scientific Reports 2017, 7: 46619. PMID: 28422190, PMCID: PMC5395958, DOI: 10.1038/srep46619.Peer-Reviewed Original ResearchNovel Role of the Mitochondrial Protein Fus1 in Protection from Premature Hearing Loss via Regulation of Oxidative Stress and Nutrient and Energy Sensing Pathways in the Inner Ear
Tan WJ, Song L, Graham M, Schettino A, Navaratnam D, Yarbrough WG, Santos-Sacchi J, Ivanova AV. Novel Role of the Mitochondrial Protein Fus1 in Protection from Premature Hearing Loss via Regulation of Oxidative Stress and Nutrient and Energy Sensing Pathways in the Inner Ear. Antioxidants & Redox Signaling 2017, 27: 489-509. PMID: 28135838, PMCID: PMC5564041, DOI: 10.1089/ars.2016.6851.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcysteineAnimalsAntioxidantsDisease Models, AnimalEar, InnerEvoked Potentials, Auditory, Brain StemGene Knockout TechniquesHearing LossHumansMiceMicroscopy, Electron, TransmissionMitochondriaOxidative StressProto-Oncogene Proteins c-aktPTEN PhosphohydrolaseSignal TransductionSpiral GanglionTOR Serine-Threonine KinasesTumor Suppressor ProteinsConceptsAge-related hearing lossAuditory brainstem responseHearing lossKO miceEndocochlear potentialOxidative stressMitochondrial dysfunctionMitochondrial dysfunction/oxidative stressEnergy sensing pathwaysNovel therapeutic strategiesMolecular mechanismsPremature hearing lossCochlear stria vascularisMajor hearing lossChronic mitochondrial dysfunctionMetabolic etiologyWorldwide epidemicBrainstem responseClinical trialsVascular pathologyTherapeutic strategiesPathological alterationsABR parametersAO treatmentStria vascularis
2013
IR Laser-Induced Perturbations of the Voltage-Dependent Solute Carrier Protein SLC26a5
Okunade O, Santos-Sacchi J. IR Laser-Induced Perturbations of the Voltage-Dependent Solute Carrier Protein SLC26a5. Biophysical Journal 2013, 105: 1822-1828. PMID: 24138858, PMCID: PMC3797594, DOI: 10.1016/j.bpj.2013.09.008.Peer-Reviewed Original ResearchReal Time Measures of Prestin Charge and Fluorescence during Plasma Membrane Trafficking Reveal Sub-Tetrameric Activity
Bian S, Navaratnam D, Santos-Sacchi J. Real Time Measures of Prestin Charge and Fluorescence during Plasma Membrane Trafficking Reveal Sub-Tetrameric Activity. PLOS ONE 2013, 8: e66078. PMID: 23762468, PMCID: PMC3677934, DOI: 10.1371/journal.pone.0066078.Peer-Reviewed Original ResearchConceptsObligate tetramerPlasma membraneMembrane motor proteinIntegral membrane proteinsTetracycline-inducible cell lineMembrane proteinsMotor proteinsPrestin densityTemperature blockPrestinFluorescence measuresMembrane fluorescenceCell linesNonlinear capacitanceCochlear amplificationProteinTetramerMembraneFluorescencePrevious observationsVoltage clampFluorescence methodCellsAmplification
2012
Mitochondrial Stress Engages E2F1 Apoptotic Signaling to Cause Deafness
Raimundo N, Song L, Shutt TE, McKay SE, Cotney J, Guan MX, Gilliland TC, Hohuan D, Santos-Sacchi J, Shadel GS. Mitochondrial Stress Engages E2F1 Apoptotic Signaling to Cause Deafness. Cell 2012, 148: 716-726. PMID: 22341444, PMCID: PMC3285425, DOI: 10.1016/j.cell.2011.12.027.Peer-Reviewed Original ResearchConceptsAltered reactive oxygen speciesReactive oxygen speciesMitochondrial ribosome functionMitochondrial disease modelTranscription factor E2F1Tissue-specific pathologyROS-dependent activationRibosome functionRRNA methylationMitochondrial stressApoptotic signalingTissue specificityMtDNA mutationsMetabolic signalingAMP kinaseMultiple tissuesMitochondrial dysfunctionOxygen speciesE2F1MethylationSignalingG cellsEnvironmental factorsApoptosisMice exhibit
2010
Patch-clamp amplifiers on a chip
Weerakoon P, Culurciello E, Yang Y, Santos-Sacchi J, Kindlmann PJ, Sigworth FJ. Patch-clamp amplifiers on a chip. Journal Of Neuroscience Methods 2010, 192: 187-192. PMID: 20637803, PMCID: PMC2978236, DOI: 10.1016/j.jneumeth.2010.06.030.Peer-Reviewed Original ResearchA highly expressing Tet-inducible cell line recapitulates in situ developmental changes in prestin's Boltzmann characteristics and reveals early maturational events
Bian S, Koo BW, Kelleher S, Santos-Sacchi J, Navaratnam DS. A highly expressing Tet-inducible cell line recapitulates in situ developmental changes in prestin's Boltzmann characteristics and reveals early maturational events. American Journal Of Physiology - Cell Physiology 2010, 299: c828-c835. PMID: 20631244, PMCID: PMC3774197, DOI: 10.1152/ajpcell.00182.2010.Peer-Reviewed Original ResearchThe remarkable cochlear amplifier
Ashmore J, Avan P, Brownell W, Dallos P, Dierkes K, Fettiplace R, Grosh K, Hackney C, Hudspeth A, Jülicher F, Lindner B, Martin P, Meaud J, Petit C, Santos-Sacchi J, Sacchi J, Canlon B. The remarkable cochlear amplifier. Hearing Research 2010, 266: 1-17. PMID: 20541061, PMCID: PMC6366996, DOI: 10.1016/j.heares.2010.05.001.Peer-Reviewed Original Research
2005
On the Effect of Prestin on the Electrical Breakdown of Cell Membranes
Navarrete EG, Santos-Sacchi J. On the Effect of Prestin on the Electrical Breakdown of Cell Membranes. Biophysical Journal 2005, 90: 967-974. PMID: 16299081, PMCID: PMC1367121, DOI: 10.1529/biophysj.105.064105.Peer-Reviewed Original ResearchConceptsTSA cellsWhole cell levelVoltage-dependent activityGuinea pig OHCsOuter hair cell motor proteinMotor proteinsPM domainsMaximum transmembrane potentialPrestin activityMembrane susceptibilityTransmembrane potentialCell membranePrestinTsA201 cellsBiophysical influencesMembrane stiffnessElectroporationCellsBasal portionSignificant resistanceMembrane capacitanceProteinElectromotilityAuditory sensitivitySusceptibility
2003
New tunes from Corti’s organ: the outer hair cell boogie rules
Santos-Sacchi J. New tunes from Corti’s organ: the outer hair cell boogie rules. Current Opinion In Neurobiology 2003, 13: 459-468. PMID: 12965294, DOI: 10.1016/s0959-4388(03)00100-4.Peer-Reviewed Original ResearchConceptsSpecial cell typesHair cellsOuter hair cell electromotilityHair cell electromotilityMolecular identificationCell typesMammalsMechanism of actionOuter hair cellsAdditional mechanismVertebratesCellsAmplificationMechanismKnockoutElectromotilityOrgansSuch amplificationCorti's organAcoustic stimuliRemarkable progress
2001
Temperature dependence of non-linear capacitance in human embryonic kidney cells transfected with prestin, the outer hair cell motor protein
Meltzer J, Santos-Sacchi J. Temperature dependence of non-linear capacitance in human embryonic kidney cells transfected with prestin, the outer hair cell motor protein. Neuroscience Letters 2001, 313: 141-144. PMID: 11682147, DOI: 10.1016/s0304-3940(01)02266-2.Peer-Reviewed Original ResearchEffects of membrane potential and tension on prestin, the outer hair cell lateral membrane motor protein
Santos‐Sacchi J, Shen W, Zheng J, Dallos P. Effects of membrane potential and tension on prestin, the outer hair cell lateral membrane motor protein. The Journal Of Physiology 2001, 531: 661-666. PMID: 11251048, PMCID: PMC2278494, DOI: 10.1111/j.1469-7793.2001.0661h.x.Peer-Reviewed Original ResearchConceptsMembrane tensionMembrane motor proteinMembrane-bound proteinsHuman embryonic kidney cellsLateral plasma membraneEmbryonic kidney cellsMolecular basisPlasma membraneProtein prestinMotor proteinsConformational changesHigh-resolution analysisPrestin activityPrestinKidney cellsMembrane potential
1995
Expression in cochlea and retina of myosin VIIa, the gene product defective in Usher syndrome type 1B.
Hasson T, Heintzelman M, Santos-Sacchi J, Corey D, Mooseker M. Expression in cochlea and retina of myosin VIIa, the gene product defective in Usher syndrome type 1B. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 9815-9819. PMID: 7568224, PMCID: PMC40893, DOI: 10.1073/pnas.92.21.9815.Peer-Reviewed Original ResearchMeSH KeywordsAbnormalities, MultipleAmino Acid SequenceAnimalsAntibody SpecificityBlindnessCochleaDeafnessDyneinsFluorescent Antibody TechniqueGuinea PigsHearing Loss, SensorineuralHumansImmunoblottingMolecular Sequence DataMyosin VIIaMyosinsRatsRetinaRetinitis PigmentosaSequence Homology, Amino AcidSwineSyndromeTissue DistributionConceptsHair cellsMyosin VIIa expressionEpithelial cellsMyosin VIIaCochlear hair cellsMyosin VIIa functionOuter hair cellsUsher syndrome type 1BMyosin VIIA geneVestibular dysfunctionCell-specific localizationCongenital deafnessRetinitis pigmentosaUsher syndromeType 1bType 1B.Normal functionApical stereociliaVIIaDeafnessDisease phenotypeCochleaInherited diseaseRetinaShaker-1