2024
Lysosomal TMEM106B interacts with galactosylceramidase to regulate myelin lipid metabolism
Takahashi H, Perez-Canamas A, Lee C, Ye H, Han X, Strittmatter S. Lysosomal TMEM106B interacts with galactosylceramidase to regulate myelin lipid metabolism. Communications Biology 2024, 7: 1088. PMID: 39237682, PMCID: PMC11377756, DOI: 10.1038/s42003-024-06810-5.Peer-Reviewed Original ResearchConceptsMyelin lipid metabolismCo-immunoprecipitation assaysSulfated derivative sulfatideLipid metabolismAssociated with multiple neurological disordersCo-immunoprecipitationTMEM106BTransmembrane proteinsAmyloid fibrilsTMEM106B deficiencyHypomyelinating leukodystrophyAlzheimer's diseasePhysiological functionsFrontotemporal dementiaMolecular levelNeurodegenerative brainGalactosylceramidaseLipidomic analysisMultiple neurological disordersMetabolismMyelin lipidsDecreased levelsEndolysosomesAmyloidGalactosylceramidase activity
2023
Concerted roles of LRRTM1 and SynCAM 1 in organizing prefrontal cortex synapses and cognitive functions
de Arce K, Ribic A, Chowdhury D, Watters K, Thompson G, Sanganahalli B, Lippard E, Rohlmann A, Strittmatter S, Missler M, Hyder F, Biederer T. Concerted roles of LRRTM1 and SynCAM 1 in organizing prefrontal cortex synapses and cognitive functions. Nature Communications 2023, 14: 459. PMID: 36709330, PMCID: PMC9884278, DOI: 10.1038/s41467-023-36042-w.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell Adhesion Molecule-1CognitionMembrane ProteinsMiceMice, KnockoutNerve Tissue ProteinsPrefrontal CortexSynapsesConceptsPrefrontal cortexDKO miceSynCAM 1Aberrant neuronal activityDendritic spine numberPrefrontal cortex synapsesSynapse organizersSynapse numberMature brainNeuronal activityKnockout miceSpine numberSynapse developmentCognitive functionTrans-synaptic complexesImmunoglobulin family membersMiceFamily membersSynapsesLRRTM1Behavioral domainsHippocampusCognitive tasksConcerted roleCortex
2020
Quantification of SV2A Binding in Rodent Brain Using [18F]SynVesT-1 and PET Imaging
Sadasivam P, Fang XT, Toyonaga T, Lee S, Xu Y, Zheng MQ, Spurrier J, Huang Y, Strittmatter SM, Carson RE, Cai Z. Quantification of SV2A Binding in Rodent Brain Using [18F]SynVesT-1 and PET Imaging. Molecular Imaging And Biology 2020, 23: 372-381. PMID: 33258040, PMCID: PMC8105262, DOI: 10.1007/s11307-020-01567-9.Peer-Reviewed Original ResearchConceptsBrain stemAlzheimer's diseaseMin postinjectionAnimal modelsAPP/PS1 miceReference regionStandardized uptake value ratioDynamic PET imaging dataUptake value ratioRodent brain tissueStatic PET scansDifferent imaging windowsPET imaging dataWild-type controlsReference tissue modelPS1 miceAD pathogenesisTherapeutic effectMouse modelRodent modelsLittermate controlsPET scansRodent brainPreclinical imaging studiesTherapeutic drug efficacy
2019
Limiting Neuronal Nogo Receptor 1 Signaling during Experimental Autoimmune Encephalomyelitis Preserves Axonal Transport and Abrogates Inflammatory Demyelination
Lee JY, Kim MJ, Thomas S, Oorschot V, Ramm G, Aui PM, Sekine Y, Deliyanti D, Wilkinson-Berka J, Niego B, Harvey AR, Theotokis P, McLean C, Strittmatter SM, Petratos S. Limiting Neuronal Nogo Receptor 1 Signaling during Experimental Autoimmune Encephalomyelitis Preserves Axonal Transport and Abrogates Inflammatory Demyelination. Journal Of Neuroscience 2019, 39: 5562-5580. PMID: 31061088, PMCID: PMC6616297, DOI: 10.1523/jneurosci.1760-18.2019.Peer-Reviewed Original ResearchMeSH KeywordsAdultAgedAged, 80 and overAnimalsAxonal TransportAxonsCells, CulturedEncephalomyelitis, Autoimmune, ExperimentalFemaleHumansIntercellular Signaling Peptides and ProteinsKinesinsMaleMiceMice, Inbred C57BLMiddle AgedMyelin SheathNerve Tissue ProteinsNogo Receptor 1Retinal Ganglion CellsSignal TransductionConceptsExperimental autoimmune encephalomyelitisCollapsin response mediator protein 2Optic nerveAxonal degenerationMultiple sclerosisAxonal vesicular transportAutoimmune encephalomyelitisInflammatory demyelinationAxonal integritySeverity of EAECre deletionAxonal transportRetinal ganglion cell axonsAxonal motor proteinsEAE-induced miceImmune-mediated destructionProgressive multiple sclerosisNeuron-specific deletionNogo receptor 1Ganglion cell axonsAnterograde transportFlx/Response mediator protein 2Adeno-associated virus serotype 2Phosphorylation of CRMP2Plexina2 and CRMP2 Signaling Complex Is Activated by Nogo-A-Liganded Ngr1 to Restrict Corticospinal Axon Sprouting after Trauma
Sekine Y, Algarate PT, Cafferty WBJ, Strittmatter SM. Plexina2 and CRMP2 Signaling Complex Is Activated by Nogo-A-Liganded Ngr1 to Restrict Corticospinal Axon Sprouting after Trauma. Journal Of Neuroscience 2019, 39: 3204-3216. PMID: 30804090, PMCID: PMC6788813, DOI: 10.1523/jneurosci.2996-18.2019.Peer-Reviewed Original ResearchConceptsCNS traumaNeural repairMouse cervical spinal cordSpinal cord traumaCervical spinal cordNon-neuronal cellsInteraction of NogoAxon growth inhibitionAxonal guidance mechanismsNeurological recoveryAxonal sproutingCNS pathwaysCord traumaFunctional recoveryAxon sproutingSpinal cordNgR1 functionUnilateral pyramidotomyAxon regenerationAdult traumaNgR1TraumaAxon growthNogoCytoplasmic mediators
2014
Lysosome size, motility and stress response regulated by fronto-temporal dementia modifier TMEM106B
Stagi M, Klein ZA, Gould TJ, Bewersdorf J, Strittmatter SM. Lysosome size, motility and stress response regulated by fronto-temporal dementia modifier TMEM106B. Molecular And Cellular Neuroscience 2014, 61: 226-240. PMID: 25066864, PMCID: PMC4145808, DOI: 10.1016/j.mcn.2014.07.006.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsCells, CulturedChlorocebus aethiopsEmbryo, MammalianGreen Fluorescent ProteinsHumansLuminescent ProteinsLysosomal-Associated Membrane Protein 1LysosomesMembrane ProteinsMiceMice, Inbred C57BLMicrotubule-Associated ProteinsNerve Tissue ProteinsProtein TransportRNA, MessengerRNA, Small InterferingStress, PhysiologicalTransfection
2012
LRRTM1-deficient mice show a rare phenotype of avoiding small enclosures—A tentative mouse model for claustrophobia-like behaviour
Voikar V, Kulesskaya N, Laakso T, Lauren J, Strittmatter SM, Airaksinen MS. LRRTM1-deficient mice show a rare phenotype of avoiding small enclosures—A tentative mouse model for claustrophobia-like behaviour. Behavioural Brain Research 2012, 238: 69-78. PMID: 23089646, PMCID: PMC3784023, DOI: 10.1016/j.bbr.2012.10.013.Peer-Reviewed Original ResearchLimiting multiple sclerosis related axonopathy by blocking Nogo receptor and CRMP-2 phosphorylation
Petratos S, Ozturk E, Azari MF, Kenny R, Lee JY, Magee KA, Harvey AR, McDonald C, Taghian K, Moussa L, Aui P, Siatskas C, Litwak S, Fehlings MG, Strittmatter SM, Bernard CC. Limiting multiple sclerosis related axonopathy by blocking Nogo receptor and CRMP-2 phosphorylation. Brain 2012, 135: 1794-1818. PMID: 22544872, PMCID: PMC3589918, DOI: 10.1093/brain/aws100.Peer-Reviewed Original ResearchMeSH KeywordsAdultAnalysis of VarianceAnimalsAntibodiesAxonsCD3 ComplexCell Line, TumorDemyelinating DiseasesDisease Models, AnimalEncephalomyelitis, Autoimmune, ExperimentalFemaleGene Expression RegulationGlycoproteinsGPI-Linked ProteinsGreen Fluorescent ProteinsHumansImmunoprecipitationIntercellular Signaling Peptides and ProteinsMaleMiceMice, Inbred C57BLMice, KnockoutMiddle AgedMultiple SclerosisMutationMyelin ProteinsMyelin-Oligodendrocyte GlycoproteinNerve DegenerationNerve Tissue ProteinsNeuroblastomaNeurofilament ProteinsNogo Receptor 1Optic NervePeptide FragmentsPhosphorylationReceptors, Cell SurfaceRetinal Ganglion CellsSeverity of Illness IndexSilver StainingSpinal CordTau ProteinsTime FactorsTransduction, GeneticTubulinConceptsExperimental autoimmune encephalomyelitisAutoimmune encephalomyelitisMyelin oligodendrocyte glycoproteinMultiple sclerosisAxonal degenerationSpinal cordChronic active multiple sclerosis lesionsOptic nerve axonal degenerationNogo-66 receptor 1CRMP-2Axonal growth inhibitorsCollapsin response mediator protein 2Improved clinical outcomesSpinal cord neuronsRetinal ganglion cellsResponse mediator protein 2Central nervous systemViable therapeutic targetAdeno-associated viral vectorMultiple sclerosis lesionsClinical outcomesOptic nerveCord neuronsOligodendrocyte glycoproteinGanglion cellsPlexinA2 limits recovery from corticospinal axotomy by mediating oligodendrocyte-derived Sema6A growth inhibition
Shim SO, Cafferty WB, Schmidt EC, Kim BG, Fujisawa H, Strittmatter SM. PlexinA2 limits recovery from corticospinal axotomy by mediating oligodendrocyte-derived Sema6A growth inhibition. Molecular And Cellular Neuroscience 2012, 50: 193-200. PMID: 22564823, PMCID: PMC3383336, DOI: 10.1016/j.mcn.2012.04.007.Peer-Reviewed Original ResearchConceptsAxonal growthSpinal cordPellet retrieval taskCervical spinal cordWild-type miceContralateral gray matterAxon guidance cuesSevered fibersSprouted fibersAxonal sproutingCorticofugal projectionsFunctional recoveryBehavioral recoveryCNS injuryImpaired forelimbClass 3 semaphorinsCorticospinal fibersCorticospinal tractMedullary pyramidsSynaptic punctaInhibitor receptorsType miceUnilateral pyramidotomyNeuron inhibitionAdult trauma
2010
MAG and OMgp Synergize with Nogo-A to Restrict Axonal Growth and Neurological Recovery after Spinal Cord Trauma
Cafferty WB, Duffy P, Huebner E, Strittmatter SM. MAG and OMgp Synergize with Nogo-A to Restrict Axonal Growth and Neurological Recovery after Spinal Cord Trauma. Journal Of Neuroscience 2010, 30: 6825-6837. PMID: 20484625, PMCID: PMC2883258, DOI: 10.1523/jneurosci.6239-09.2010.Peer-Reviewed Original ResearchMeSH KeywordsAnalysis of VarianceAnimalsBiotinCells, CulturedDextransDisease Models, AnimalFemaleFunctional LateralityGanglia, SpinalGPI-Linked ProteinsMaleMiceMice, Inbred C57BLMice, KnockoutMutationMyelin ProteinsMyelin-Associated GlycoproteinMyelin-Oligodendrocyte GlycoproteinNerve Tissue ProteinsNeuronsNogo ProteinsPyramidal TractsReceptors, Cell SurfaceReceptors, SerotoninRecovery of FunctionSpinal Cord InjuriesConceptsAxonal growthSpinal Cord Injury StudyMutant miceGreater axonal growthGreater behavioral recoverySpinal cord traumaWild-type miceAxonal growth inhibitionHeterozygous mutant miceDeficient myelinNeurological recoveryCNS damageTriple-mutant miceBehavioral recoveryCord traumaFunctional recoveryNeurological functionMyelin inhibitorsAxonal regrowthReceptor mechanismsInjury studiesMyelin inhibitionDecoy receptorOptimal chanceMice
2009
LGI1-associated epilepsy through altered ADAM23-dependent neuronal morphology
Owuor K, Harel NY, Englot DJ, Hisama F, Blumenfeld H, Strittmatter SM. LGI1-associated epilepsy through altered ADAM23-dependent neuronal morphology. Molecular And Cellular Neuroscience 2009, 42: 448-457. PMID: 19796686, PMCID: PMC2783222, DOI: 10.1016/j.mcn.2009.09.008.Peer-Reviewed Original ResearchConceptsNeuronal morphologyAutosomal dominant partial epilepsyCA1 pyramidal neuronsSeizure thresholdSpontaneous seizuresPartial epilepsyPyramidal neuronsDendritic arborizationLGI1PSD-95LGI1 geneEpilepsy genesADAM23ADPEAFADAM22EpilepsyNeurite outgrowthIon channelsBrain genesUnbiased screenAuditory featuresOutgrowthSeizuresArborizationRelated proteins
2008
Release of MICAL Autoinhibition by Semaphorin-Plexin Signaling Promotes Interaction with Collapsin Response Mediator Protein
Schmidt EF, Shim SO, Strittmatter SM. Release of MICAL Autoinhibition by Semaphorin-Plexin Signaling Promotes Interaction with Collapsin Response Mediator Protein. Journal Of Neuroscience 2008, 28: 2287-2297. PMID: 18305261, PMCID: PMC2846290, DOI: 10.1523/jneurosci.5646-07.2008.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCell Adhesion MoleculesCell Line, TransformedChick EmbryoCytoskeletal ProteinsFlavin-Adenine DinucleotideGanglia, SpinalGenetic VectorsHIVHumansImmunoprecipitationIntracellular Signaling Peptides and ProteinsLIM Domain ProteinsMembrane GlycoproteinsMicrofilament ProteinsMixed Function OxygenasesMutationNerve Tissue ProteinsNeuritesNeuronsPeptide FragmentsProtein BindingSemaphorin-3ASemaphorinsSignal TransductionTransfectionConceptsCollapsin response mediator proteinsMediator proteinsCytoplasmic proteinsEnzymatic domainsCatalytic domainPlexin functionPlexin receptorsTerminal domainMICALPromotes interactionAxon guidanceNeuronal developmentAxonal guidanceEnzymatic activityProteinAutoinhibitionDomainPlexinsSignalingSemaphorinsActivatorAssociatesInteractionActivityActivation
2007
The reticulons: a family of proteins with diverse functions
Yang YS, Strittmatter SM. The reticulons: a family of proteins with diverse functions. Genome Biology 2007, 8: 234. PMID: 18177508, PMCID: PMC2246256, DOI: 10.1186/gb-2007-8-12-234.Peer-Reviewed Original ResearchConceptsDiverse functionsEndoplasmic reticulum-Golgi traffickingReticulon homology domainMembrane-associated proteinsAmino-terminal domainFamily of proteinsEukaryotic kingdomsMembrane morphogenesisHomology domainHydrophilic loopReticulon 4Reticulon familyReticulonsDiversity of structuresExpression patternsVesicle formationEndoplasmic reticulumAmino acidsCell surfaceHydrophobic regionAxon growthDiverse groupNeurodegenerative diseasesProteinAmyotrophic lateral sclerosisNo association between schizophrenia and polymorphisms of the PlexinA2 gene in Chinese Han Trios
Budel S, Shim SO, Feng Z, Zhao H, Hisama F, Strittmatter SM. No association between schizophrenia and polymorphisms of the PlexinA2 gene in Chinese Han Trios. Schizophrenia Research 2007, 99: 365-366. PMID: 18096369, PMCID: PMC2276648, DOI: 10.1016/j.schres.2007.10.033.Peer-Reviewed Original ResearchROCK and Rho: Biochemistry and Neuronal Functions of Rho-Associated Protein Kinases
Schmandke A, Schmandke A, Strittmatter SM. ROCK and Rho: Biochemistry and Neuronal Functions of Rho-Associated Protein Kinases. The Neuroscientist 2007, 13: 454-469. PMID: 17901255, PMCID: PMC2849133, DOI: 10.1177/1073858407303611.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell Adhesion MoleculesCentral Nervous SystemCytoskeletonHumansLipoproteinsMyelin ProteinsNerve Tissue ProteinsNeuronsNogo ProteinsProtein Processing, Post-TranslationalReceptor Protein-Tyrosine KinasesReceptors, G-Protein-CoupledReceptors, ImmunologicRho GTP-Binding ProteinsRho-Associated KinasesSignal TransductionConceptsProtein kinaseRho-Associated Protein KinaseSignal transduction mechanismsNeuronal functionDiverse neuronal functionsActin cytoskeletonRho familyExtracellular signalsROCK functionSignaling pathwaysBiochemical knowledgeCell survivalTransduction mechanismsCell migrationAxonal guidanceDendritic spine morphologyKinaseROCK pathwayPathwayNeuronal regenerationSpine morphologyRhoBrain developmentKey rolePotential sitesLRRTM1 on chromosome 2p12 is a maternally suppressed gene that is associated paternally with handedness and schizophrenia
Francks C, Maegawa S, Laurén J, Abrahams BS, Velayos-Baeza A, Medland SE, Colella S, Groszer M, McAuley EZ, Caffrey TM, Timmusk T, Pruunsild P, Koppel I, Lind PA, Matsumoto-Itaba N, Nicod J, Xiong L, Joober R, Enard W, Krinsky B, Nanba E, Richardson AJ, Riley BP, Martin NG, Strittmatter SM, Möller HJ, Rujescu D, St Clair D, Muglia P, Roos JL, Fisher SE, Wade-Martins R, Rouleau GA, Stein JF, Karayiorgou M, Geschwind DH, Ragoussis J, Kendler KS, Airaksinen MS, Oshimura M, DeLisi LE, Monaco AP. LRRTM1 on chromosome 2p12 is a maternally suppressed gene that is associated paternally with handedness and schizophrenia. Molecular Psychiatry 2007, 12: 1129-1139. PMID: 17667961, PMCID: PMC2990633, DOI: 10.1038/sj.mp.4002053.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrainCell Line, TransformedChromosomes, Human, Pair 2Family HealthFemaleFunctional LateralityGene Expression Regulation, DevelopmentalGenetic Predisposition to DiseaseGenotypeHumansIn Situ HybridizationKaryotypingMaleMembrane ProteinsMiceNerve Tissue ProteinsSchizophreniaSubcellular FractionsConceptsHuman brain asymmetryPutative genetic effectsEvolutionary originImprinted genesChromosome 2p12Candidate genesBehavioral evolutionHuman handednessNeuronal differentiationBrain asymmetryLRRTM1Specific forebrain structuresSchizophrenia/schizoaffective disorderGenetic effectsGenesSame haplotypePotential genetic influencesDirect confirmatory evidenceCommon neurodevelopmental disorderFunction underliesForebrain structuresSchizoaffective disorderHaplotypesSignificant associationNeuropsychiatric disordersThe CRMP Family of Proteins and Their Role in Sema3A Signaling
Schmidt EF, Strittmatter SM. The CRMP Family of Proteins and Their Role in Sema3A Signaling. Advances In Experimental Medicine And Biology 2007, 600: 1-11. PMID: 17607942, PMCID: PMC2853248, DOI: 10.1007/978-0-387-70956-7_1.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsGrowth ConesHumansNerve Tissue ProteinsProtein IsoformsSemaphorin-3ASignal TransductionConceptsMonomeric G proteinsLarge intracellular domainNeuropilin-1Class A plexinsRepulsive axon guidance cuesCurrent knowledgeSema3A signalingVertebrate semaphorinsAxon guidance cuesCellular processesSignal transductionBinding partnerIntracellular domainMediator proteinsProtein turnoverCRMP proteinsF-actinCellular responsesCytosolic phosphoproteinG proteinsNeuronal differentiationRedox proteinsReceptor complexCellular effectsCell membrane
2006
Characterization of Myelin Ligand Complexes with Neuronal Nogo-66 Receptor Family Members*
Lauré;n J, Hu F, Chin J, Liao J, Airaksinen MS, Strittmatter SM. Characterization of Myelin Ligand Complexes with Neuronal Nogo-66 Receptor Family Members*. Journal Of Biological Chemistry 2006, 282: 5715-5725. PMID: 17189258, PMCID: PMC2852886, DOI: 10.1074/jbc.m609797200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionAnimalsAxonsCentral Nervous SystemChlorocebus aethiopsCOS CellsGPI-Linked ProteinsHumansLectinsLigandsModels, MolecularMyelin ProteinsMyelin-Associated GlycoproteinNeoplasm ProteinsNerve Tissue ProteinsNogo Receptor 1Protein BindingProtein Structure, TertiaryReceptors, Cell SurfaceRegenerationRanBPM Contributes to Semaphorin3A Signaling through Plexin-A Receptors
Togashi H, Schmidt EF, Strittmatter SM. RanBPM Contributes to Semaphorin3A Signaling through Plexin-A Receptors. Journal Of Neuroscience 2006, 26: 4961-4969. PMID: 16672672, PMCID: PMC2846289, DOI: 10.1523/jneurosci.0704-06.2006.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCell Adhesion MoleculesCell DeathCell SizeCells, CulturedChick EmbryoCloning, MolecularCricetinaeCricetulusCytoskeletal ProteinsDose-Response Relationship, DrugDrug InteractionsEnzyme InhibitorsGanglia, SpinalGene ExpressionGreen Fluorescent ProteinsHumansImmunoprecipitationIn Situ Nick-End LabelingNerve Tissue ProteinsNeuritesNeuronsNeuropilin-1Nuclear ProteinsRan GTP-Binding ProteinSemaphorin-3ASignal TransductionTranscription Factor AP-1TransfectionTwo-Hybrid System TechniquesConceptsPlexin-A1Collapsin response mediator proteinsNervous system developmentReceptor complex consistingSignal transductionRanBPMMediator proteinsMicrotubule functionCell spreadingComplex consistingAxonal guidanceNeuronal cellsAxonal guidance cuesProteinGuidance cuesPlexinsAxonal outgrowthExpressionSema3ATransductionReceptorsDomainOverexpressionNeuropilinsSystem development
2004
Regulating axon growth within the postnatal central nervous system
Hu F, Strittmatter SM. Regulating axon growth within the postnatal central nervous system. Seminars In Perinatology 2004, 28: 371-378. PMID: 15693393, DOI: 10.1053/j.semperi.2004.10.001.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsCentral Nervous SystemGPI-Linked ProteinsGrowth InhibitorsHumansHypoxiaIntracellular Signaling Peptides and ProteinsMembrane ProteinsMiceMyelin ProteinsMyelin-Associated GlycoproteinMyelin-Oligodendrocyte GlycoproteinNerve RegenerationNerve Tissue ProteinsNogo ProteinsNogo Receptor 1Receptor, Nerve Growth FactorReceptors, Cell SurfaceConceptsCentral nervous systemAxonal growthNervous systemNeuronal developmentAdult central nervous systemMature central nervous systemAxon growth inhibitorsPostnatal central nervous systemPotential therapeutic interventionsNew neuronal connectionsMyelin-derived proteinsAxonal sproutingDirect blockadeNgR proteinPostnatal brainNeuronal connectionsTherapeutic interventionsAxon growthDevelopmental hypoxiaReduced expressionMyelin proteinsHypoxic conditionsInhibitor pathwayImportant investigationCritical role