2023
Multi-omics identifies large mitoribosomal subunit instability caused by pathogenic MRPL39 variants as a cause of pediatric onset mitochondrial disease
Amarasekera S, Hock D, Lake N, Calvo S, Grønborg S, Krzesinski E, Amor D, Fahey M, Simons C, Wibrand F, Mootha V, Lek M, Lunke S, Stark Z, Østergaard E, Christodoulou J, Thorburn D, Stroud D, Compton A. Multi-omics identifies large mitoribosomal subunit instability caused by pathogenic MRPL39 variants as a cause of pediatric onset mitochondrial disease. Human Molecular Genetics 2023, 32: 2441-2454. PMID: 37133451, PMCID: PMC10360397, DOI: 10.1093/hmg/ddad069.Peer-Reviewed Original ResearchConceptsQuantitative proteomicsMitochondrial oxidative phosphorylation systemProtein complex assemblySmall mitoribosomal subunitExome sequencingOxidative phosphorylation systemMitochondrial deoxyribonucleic acidMitochondrial ribosomesMitoribosomal subunitDeoxyribonucleic acidGene-disease associationsLarge subunitOXPHOS disordersSmall subunitComplex assemblyPhosphorylation systemProteomic dataComplex abundanceFunctional validationDisease genesGenome sequencingMitochondrial diseaseCryptic exonGene matchingProtein signatures
2017
Biallelic Mutations in MRPS34 Lead to Instability of the Small Mitoribosomal Subunit and Leigh Syndrome
Lake N, Webb B, Stroud D, Richman T, Ruzzenente B, Compton A, Mountford H, Pulman J, Zangarelli C, Rio M, Boddaert N, Assouline Z, Sherpa M, Schadt E, Houten S, Byrnes J, McCormick E, Zolkipli-Cunningham Z, Haude K, Zhang Z, Retterer K, Bai R, Calvo S, Mootha V, Christodoulou J, Rötig A, Filipovska A, Cristian I, Falk M, Metodiev M, Thorburn D. Biallelic Mutations in MRPS34 Lead to Instability of the Small Mitoribosomal Subunit and Leigh Syndrome. American Journal Of Human Genetics 2017, 101: 239-254. PMID: 28777931, PMCID: PMC5544391, DOI: 10.1016/j.ajhg.2017.07.005.Peer-Reviewed Original ResearchConceptsSmall mitoribosomal subunitMitoribosomal subunitHuman oxidative phosphorylation (OXPHOS) systemMitochondrial protein translationOxidative phosphorylation systemMitochondrial translation defectQuantitative proteomic analysisSpecific cellular pathwaysLeigh syndromeLentiviral-mediated expressionMitoribosomal proteinsMitochondrial ribosomesOXPHOS subunitsMitochondrial translationOXPHOS defectsProtein translationMitochondrial DNATranslation defectsUnrelated familiesProteomic analysisPhosphorylation systemQuantitative proteomicsCellular pathwaysProtein subunitsSubunit proteins
1996
Ca2+ stimulates both the respiratory and phosphorylation subsystems in rat heart mitochondria
MILDAZIENE V, BANIENE R, NAUCIENE Z, MARCINKEVICIUTE A, MORKUNIENE R, BORUTAITE V, KHOLODENKO B, BROWN G. Ca2+ stimulates both the respiratory and phosphorylation subsystems in rat heart mitochondria. Biochemical Journal 1996, 320: 329-334. PMID: 8947505, PMCID: PMC1217935, DOI: 10.1042/bj3200329.Peer-Reviewed Original ResearchConceptsPhosphorylation systemPhosphorylation subsystemProton leakRat heart mitochondriaMitochondrial membrane potentialHeart mitochondriaIsolated rat heart mitochondriaOxidative phosphorylationRespiratory chainMitochondrial respirationStimulation of respirationSuccinate oxidationMembrane potentialPhosphorylationMitochondriaRespiration rateRespirationPhysiological concentrationsRespiratory subsystemState 3Ca2Free Ca2
1990
General assay for phosphoproteins in cerebrospinal fluid: A candidate market for paraneoplastic cerebellar degeneration
Gandy S, Grebb J, Rosen N, Albert K, Devinsky O, Blumberg H, Anderson N, Cedarbaum J, Porter R, Sedvall G, Posner J, Greengard P. General assay for phosphoproteins in cerebrospinal fluid: A candidate market for paraneoplastic cerebellar degeneration. Annals Of Neurology 1990, 28: 829-833. PMID: 2285268, DOI: 10.1002/ana.410280616.Peer-Reviewed Original ResearchConceptsProtein kinase C substrate proteinProtein kinase substratesProtein phosphorylation systemsSubstrate proteinsKinase substratePhosphorylation systemBiochemical characterizationCell typesPhosphoproteinNeuronal cellsNeuronal diseasesNeuronal enrichmentGeneral assayUnique markerPotential insightsNeuronal populationsProteinNeurological diseasesCerebellar degenerationCellsAssaysEnrichmentAssay techniquesKdMarkers
1989
Multisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: Peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms
Walaas S, Nairn A. Multisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: Peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms. Journal Of Molecular Neuroscience 1989, 1: 117-127. DOI: 10.1007/bf02918897.Peer-Reviewed Original ResearchCalcium/phospholipid-dependent protein kinasePhospholipid-dependent protein kinaseCalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIProtein kinaseCalcium/calmodulinProtein kinase IIKinase IICyclic AMP-dependent protein kinaseAMP-dependent protein kinaseCommon phosphorylation sitesOnly serine residuesProtein 2Cyclic AMPMultisite phosphorylationThreonine residuesPhosphorylation sitesSerine residuesPhosphorylation systemPhosphorylation mechanismCytoskeletal proteinsMAP-2KinasePeptide mapsDistinct sitesMultisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: Peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms
Ivar Walaas S, Nairn A. Multisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: Peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms. Journal Of Molecular Neuroscience 1989, 1: 117-127. PMID: 2561875, DOI: 10.1007/bf02896895.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino AcidsAnimalsBrainCalcium-Calmodulin-Dependent Protein KinasesElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelMicrotubule-Associated ProteinsOrgan SpecificityPeptide MappingPhosphopeptidesPhosphorylationProtein Kinase CProtein KinasesRatsConceptsCalcium/phospholipid-dependent protein kinasePhospholipid-dependent protein kinaseCalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIProtein kinaseCalcium/calmodulinProtein kinase IIKinase IICyclic AMP-dependent protein kinaseAMP-dependent protein kinaseCommon phosphorylation sitesOnly serine residuesProtein 2Cyclic AMPMultisite phosphorylationThreonine residuesPhosphorylation sitesSerine residuesPhosphorylation systemPhosphorylation mechanismCytoskeletal proteinsMAP-2KinasePeptide mapsDistinct sites
1988
Skeletal muscle sarcolemma proteins as targets for adenosine 3′:5′-monophosphate-dependent and calcium-dependent protein kinases
Walaas S, Horn R, Nairn A, Walaas O, Adler A. Skeletal muscle sarcolemma proteins as targets for adenosine 3′:5′-monophosphate-dependent and calcium-dependent protein kinases. Archives Of Biochemistry And Biophysics 1988, 262: 245-258. PMID: 3355169, DOI: 10.1016/0003-9861(88)90186-5.Peer-Reviewed Original ResearchConceptsCalcium-dependent protein kinaseProtein kinaseProtein phosphorylationPhosphorylation systemRat skeletal muscle plasma membranesCGMP-dependent protein kinaseIntrinsic membrane proteinsProtein phosphorylation systemsSkeletal muscle cellsSkeletal muscle plasma membranesSarcolemma proteinsMembrane proteinsProtein speciesMuscle plasma membranePlasma membraneMembrane targetsSpecific substratesKinaseMultiple hormonesDistinct setsProteinPhosphoproteinMuscle cellsPhosphorylationReticulum fractions
1986
Protein phosphorylation in cultured endothelial cells
Mackie K, Lai Y, Nairn A, Greengard P, Pitt B, Lazo J. Protein phosphorylation in cultured endothelial cells. Journal Of Cellular Physiology 1986, 128: 367-374. PMID: 3745280, DOI: 10.1002/jcp.1041280304.Peer-Reviewed Original ResearchConceptsCalcium/calmodulin-dependent protein kinaseCalmodulin-dependent protein kinaseCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseProtein kinase activityProtein kinaseKinase activityCyclic GMP-dependent protein kinase activityRespective substrate proteinsProtein phosphorylation systemsProtein kinase CSubstrate proteinsProtein phosphorylationPhosphorylation systemEndothelial cellsNumerous substratesTyrosine kinaseKinase CPulmonary artery endothelial cellsKinaseCultured endothelial cellsArtery endothelial cellsSimilar culture conditionsCulture conditionsCells
1985
Identification of calmodulin-dependent protein kinase III and its major Mr 100,000 substrate in mammalian tissues.
Nairn A, Bhagat B, Palfrey H. Identification of calmodulin-dependent protein kinase III and its major Mr 100,000 substrate in mammalian tissues. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 7939-7943. PMID: 3906654, PMCID: PMC390885, DOI: 10.1073/pnas.82.23.7939.Peer-Reviewed Original ResearchConceptsCaM-dependent protein kinaseCaM kinase IIIKinase IIIProtein kinaseMammalian tissuesCalmodulin-dependent protein kinase IIIProtein kinase IIIDependent protein kinaseProtein phosphorylation systemsWidespread tissue distributionTotal cytosolic proteinAnimal cellsPhosphorylation systemSubstrate specificityCytosolic proteinsMyosin light chainMajor substrateKinaseProteinSynapsin IPoor substrateCell linesPhosphorylase bMajor MrPolyclonal antibodies
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