2017
Bidirectional regulation of Aβ levels by Presenilin 1
Bustos V, Pulina MV, Kelahmetoglu Y, Sinha SC, Gorelick FS, Flajolet M, Greengard P. Bidirectional regulation of Aβ levels by Presenilin 1. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: 7142-7147. PMID: 28533411, PMCID: PMC5502639, DOI: 10.1073/pnas.1705235114.Peer-Reviewed Original ResearchConceptsAmyloid precursor proteinAβ levelsΓ-secretase complexAlzheimer's diseasePresenilin 1Pathogenesis of ADAβ peptidesEndogenous kinaseΒ-amyloid peptidePS1 functionIntramembranous proteinsCatalytic subunitΓ-secretase activityPlaque loadC-terminal fragmentAutophagic degradationPotential therapySer367Selective phosphorylationSequential proteolysisTransgenic micePhosphorylationCultured cellsΒ-secretaseDiseasePhosphorylated Presenilin 1 decreases β-amyloid by facilitating autophagosome–lysosome fusion
Bustos V, Pulina MV, Bispo A, Lam A, Flajolet M, Gorelick FS, Greengard P. Phosphorylated Presenilin 1 decreases β-amyloid by facilitating autophagosome–lysosome fusion. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: 7148-7153. PMID: 28533369, PMCID: PMC5502640, DOI: 10.1073/pnas.1705240114.Peer-Reviewed Original Research
2013
Tumor protein D52 controls trafficking of an apical endolysosomal secretory pathway in pancreatic acinar cells
Messenger SW, Thomas DD, Falkowski MA, Byrne JA, Gorelick FS, Groblewski GE. Tumor protein D52 controls trafficking of an apical endolysosomal secretory pathway in pancreatic acinar cells. AJP Gastrointestinal And Liver Physiology 2013, 305: g439-g452. PMID: 23868405, PMCID: PMC3761242, DOI: 10.1152/ajpgi.00143.2013.Peer-Reviewed Original ResearchConceptsImmature secretory granulesApical exocytosisTumor protein D52Endosomal compartmentsEndolysosomal compartmentsMinor regulated pathwayZymogen granule formationAcinar cellsEndosomal intermediatesISG maturationSerine 136Phosphorylation sitesTrans-GolgiSecretory pathwayAspartate substitutionContent proteinsRegulatory proteinsBrefeldin ASynaptotagmin-1Molecular componentsPancreatic acinar cellsGranule formationExocytosisLysosomal membraneLAMP1
2012
Cerulein hyperstimulation decreases AMP-activated protein kinase levels at the site of maximal zymogen activation
Shugrue C, Alexandre M, de Villalvilla A, Kolodecik TR, Young LH, Gorelick FS, Thrower EC. Cerulein hyperstimulation decreases AMP-activated protein kinase levels at the site of maximal zymogen activation. AJP Gastrointestinal And Liver Physiology 2012, 303: g723-g732. PMID: 22821946, PMCID: PMC3468535, DOI: 10.1152/ajpgi.00082.2012.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAminoimidazole CarboxamideAMP-Activated Protein KinasesAnimalsCells, CulturedCeruletideCyclic AMP-Dependent Protein KinasesEnzyme PrecursorsGene Expression RegulationMaleMetforminOctoxynolPancreasPhosphorylationPyrazolesPyrimidinesRatsRats, Sprague-DawleyRibonucleotidesSodium Dodecyl SulfateConceptsAdenosine monophosphate-activated protein kinaseZymogen activationAMPK activityPancreatic acinar cellsMonophosphate-activated protein kinaseVacuolar ATPase activityAMPK levelsDigestive enzyme zymogensAMPK effectsProtein kinaseProtein kinase levelsE subunitAcinar cellsTime-dependent translocationCompound CCellular modelPancreatitis responsesATPase activityDifferential centrifugationPremature activationChymotrypsin activityActivationInitiating eventSoluble fractionCerulein hyperstimulation
1995
Calmodulin-dependent protein kinases in rat glioblastoma.
Cheng EH, Gorelick FS, Czernik AJ, Bagaglio DM, Hait WN. Calmodulin-dependent protein kinases in rat glioblastoma. Molecular Cancer Research 1995, 6: 615-21. PMID: 7647041.Peer-Reviewed Original ResearchConceptsCaM-dependent protein kinaseProtein kinaseKinase II activitySignal transductionCaM kinase II activityKinase IICalmodulin-dependent protein kinaseCalcium-dependent signal transductionCaM-dependent protein kinase IIExogenous synapsin ICell cycle regulationII activityCaM kinase IIIElongation factor 2Protein kinase IICell linesCaM kinase IINumerous malignant cell linesSpecific peptide substratePhosphopeptide mappingKinase IIIAbnormal cell growthCycle regulationKinase activityKinase
1994
Antibodies to an epitope on synapsin I detect a protein associated with the endocytic compartment in non-neuronal cells.
Matovcik LM, Karapetian O, Czernik AJ, Marino CR, Kinder BK, Gorelick FS. Antibodies to an epitope on synapsin I detect a protein associated with the endocytic compartment in non-neuronal cells. European Journal Of Cell Biology 1994, 65: 327-40. PMID: 7536673.Peer-Reviewed Original ResearchConceptsClone 9 cellsEndocytic compartmentsPotential substrate proteinsDependent protein kinase IISynapsin ISmall intracellular vesiclesProtein kinase IIRat liver endosomesSubstrate proteinsPhosphorylation sequenceNon-neuronal cellsCLIP-170Intracellular vesiclesKinase IILarge endosomesPostnuclear supernatantEndosomesSensitive compartmentLiver endosomesProteinConfocal microscopyCell linesVesiclesIntestinal enterocytesCompartments
1993
Phosphorylation of elongation factor 2 in normal and malignant rat glial cells.
Bagaglio DM, Cheng EH, Gorelick FS, Mitsui K, Nairn AC, Hait WN. Phosphorylation of elongation factor 2 in normal and malignant rat glial cells. Cancer Research 1993, 53: 2260-4. PMID: 8485712.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCalcium-Calmodulin-Dependent Protein KinasesCalmodulinCell DivisionCells, CulturedElongation Factor 2 KinaseGliomaMaleNeurogliaPeptide Elongation Factor 2Peptide Elongation FactorsPhosphorylationPrecipitin TestsProtein KinasesRatsRats, Sprague-DawleyTrifluoperazineTumor Cells, CulturedConceptsRat brain white matterNormal glial tissueGlial tissueGlioma cellsC6 cellsC6 rat glioma cellsCaM kinase IIIRat glial cellsFactor 2Rat glioma cellsBrain white matterNormal gliaElongation factor 2Glial cellsRat brainWhite matterTumor tissueBasal levelsIII activityCellular proliferationTissueDependent proteinsCellsEndogenous substratesHomogenatesDistribution of calcium/calmodulin-dependent protein kinase II in rat ileal enterocytes
Matovcik LM, Haimowitz B, Goldenring JR, Czernik AJ, Gorelick FS. Distribution of calcium/calmodulin-dependent protein kinase II in rat ileal enterocytes. American Journal Of Physiology 1993, 264: c1029-c1036. PMID: 8386447, DOI: 10.1152/ajpcell.1993.264.4.c1029.Peer-Reviewed Original ResearchConceptsProtein kinase IIDependent protein kinase IIKinase IICalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIDependent kinase activityRelative molecular massSpecific peptide inhibitorWide tissue distributionTerminal web regionIntestinal epithelial cellsEpithelial cytoskeletonKinase activityMyosin IISoluble subcellular fractionMolecular massRat ilealRat ileumMultiple substratesEnterocyte cytoskeletonImmunoreactive proteinMajor effectorPeptide inhibitorEpithelial cellsTissue distribution
1992
Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is a binding protein for synapsin I
Benfenati F, Valtorta F, Rubenstein J, Gorelick F, Greengard P, Czernik A. Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is a binding protein for synapsin I. Nature 1992, 359: 417-420. PMID: 1328883, DOI: 10.1038/359417a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrainCalcium-Calmodulin-Dependent Protein KinasesChromatography, High Pressure LiquidElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelGene Expression Regulation, EnzymologicMolecular Sequence DataPhosphorylationProtein KinasesRatsReceptors, NeurotransmitterSubstrate SpecificitySynapsinsSynaptic VesiclesConceptsDependent protein kinase IIProtein kinase IIC-terminal regionKinase IISynapsin ISynaptic vesicle-associated phosphoproteinsAmino-terminal regionCarboxy-terminal regionKinase functionRegulatory domainProtein componentsMembrane phospholipidsProteinPhosphoproteinVesiclesEnzymeRegionBindingPhospholipidsDomainSynaptic
1991
Agonist-regulated phosphorylation of the pancreatic cholecystokinin receptor
Klueppelberg UG, Gates LK, Gorelick FS, Miller LJ. Agonist-regulated phosphorylation of the pancreatic cholecystokinin receptor. Journal Of Biological Chemistry 1991, 266: 2403-2408. PMID: 1989991, DOI: 10.1016/s0021-9258(18)52258-4.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCarbacholCell FractionationChromatography, AffinityChromatography, High Pressure LiquidElectrophoresis, Polyacrylamide GelEnzyme ActivationKineticsMalePancreasPhosphorylationProtein Kinase CRatsRats, Inbred StrainsReceptors, CholecystokininSincalideSolubilityTetradecanoylphorbol AcetateConceptsC activationSodium dodecyl sulfate-polyacrylamide gelsDodecyl sulfate-polyacrylamide gelsProtein kinase C activationPlasma membrane glycoproteinsPhosphorylated MrKinase C activationSulfate-polyacrylamide gelsSerine residuesRegulated mannerAffinity-labeled proteinsMembrane glycoproteinsPhosphorylationReceptor proteinProteinNative formATP poolAffinity resinLectin affinity chromatographyConcentration-dependent mannerDirect activationPancreatic cholecystokinin receptorSubsequent solubilizationReceptorsActivation
1990
Regulated phosphorylation of secretory granule membrane proteins of the rat parotid gland
Marino CR, Castle JD, Gorelick FS. Regulated phosphorylation of secretory granule membrane proteins of the rat parotid gland. American Journal Of Physiology 1990, 259: g70-g77. PMID: 1695488, DOI: 10.1152/ajpgi.1990.259.1.g70.Peer-Reviewed Original ResearchConceptsSecretory granule membrane proteinsIntegral membrane proteinsMembrane proteinsGranule membrane proteinProtein phosphorylation eventsGranule membrane fractionExocrine secretory granulesPhosphorylation eventsSodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisRat parotid glandRegulated phosphorylationSulfate-polyacrylamide gel electrophoresisSitu phosphorylationIntact cellsMembrane fractionTime-dependent mannerPhosphorylationProteinSecretory granule fractionParotid lobulesGel electrophoresisProtein antiserumSecretory granulesPhosphoprotein
1989
Translocation of synapsin I in response to depolarization of isolated nerve terminals.
Sihra TS, Wang JK, Gorelick FS, Greengard P. Translocation of synapsin I in response to depolarization of isolated nerve terminals. Proceedings Of The National Academy Of Sciences Of The United States Of America 1989, 86: 8108-8112. PMID: 2510160, PMCID: PMC298224, DOI: 10.1073/pnas.86.20.8108.Peer-Reviewed Original ResearchConceptsSynapsin INerve terminalsRelease of neurotransmittersDepolarization of synaptosomesSmall synaptic vesiclesNeurotransmitter releaseSynaptic vesiclesDependent mannerIncubation mediumNerve terminal phosphoproteinDepolarizationPresent studyPhosphorylation stateCytosolic fractionPresence of Ca2TranslocationCa2Particulate fraction
1988
Cell-specific localization of the alpha-subunit of calcium/calmodulin-dependent protein kinase II in Purkinje cells in rodent cerebellum.
Walaas SI, Lai Y, Gorelick FS, DeCamilli P, Moretti M, Greengard P. Cell-specific localization of the alpha-subunit of calcium/calmodulin-dependent protein kinase II in Purkinje cells in rodent cerebellum. Brain Research 1988, 464: 233-42. PMID: 2850084, DOI: 10.1016/0169-328x(88)90029-0.Peer-Reviewed Original ResearchConceptsCalmodulin-dependent protein kinase type IICalcium/calmodulin-dependent protein kinase type IIProtein kinase type IIKinase type IICalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIDistinct isozymic formsProtein kinase IINormal rat cerebellumPurkinje cellsBeta/betaNon-Purkinje cellsKinase IIAlpha subunitCell-specific localizationRestricted localizationRodent cerebellumIsozymic formsDifferent cellsImmunocytochemical analysisMutant miceSubunitsType IICellsCerebellumAutophosphorylation and activation of Ca2+/calmodulin-dependent protein kinase II in intact nerve terminals.
Gorelick FS, Wang JK, Lai Y, Nairn AC, Greengard P. Autophosphorylation and activation of Ca2+/calmodulin-dependent protein kinase II in intact nerve terminals. Journal Of Biological Chemistry 1988, 263: 17209-17212. PMID: 2846557, DOI: 10.1016/s0021-9258(19)77816-8.Peer-Reviewed Original ResearchConceptsDependent protein kinase IIKinase IIAlpha subunitProtein kinase IIKinase II activityTwo-dimensional phosphopeptide mapsII activityState of phosphorylationAutophosphorylation mechanismThreonine residuesPhosphothreonine contentPhosphopeptide mapsTransient phosphorylationIndependent speciesPhosphoserine contentIntact nerve terminalsBeta subunitEnhanced phosphorylationSubunitsPhosphorylationAutophosphorylationIntact synaptosomesBasal incubation conditionsPhosphopeptidesDepolarization of synaptosomesCa2+/calmodulin-dependent protein kinase II: identification of threonine-286 as the autophosphorylation site in the alpha subunit associated with the generation of Ca2+-independent activity.
Thiel G, Czernik AJ, Gorelick F, Nairn AC, Greengard P. Ca2+/calmodulin-dependent protein kinase II: identification of threonine-286 as the autophosphorylation site in the alpha subunit associated with the generation of Ca2+-independent activity. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 6337-6341. PMID: 2842767, PMCID: PMC281965, DOI: 10.1073/pnas.85.17.6337.Peer-Reviewed Original ResearchConceptsBeta/beta' subunitsAlpha subunitThr-286Beta subunitDependent protein kinase IIProtein kinase IIAutophosphorylation sitesThreonine residuesMajor phosphopeptideNaDodSO4/PAGEPhosphorylated residuesCyanogen bromide peptidesConsensus sequenceKinase IIIndependent activityThermolytic phosphopeptidesPrimary structureGas-phase Edman degradationGeneration of Ca2Edman degradationAutophosphorylationSubunitsThreonine-286Amino acidsAsp-Xaa
1987
Ca2+/calmodulin-dependent protein kinase II: identification of autophosphorylation sites responsible for generation of Ca2+/calmodulin-independence.
Lai Y, Nairn AC, Gorelick F, Greengard P. Ca2+/calmodulin-dependent protein kinase II: identification of autophosphorylation sites responsible for generation of Ca2+/calmodulin-independence. Proceedings Of The National Academy Of Sciences Of The United States Of America 1987, 84: 5710-5714. PMID: 3475699, PMCID: PMC298932, DOI: 10.1073/pnas.84.16.5710.Peer-Reviewed Original ResearchPurification and properties of a multifunctional calcium/calmodulin-dependent protein kinase from rat pancreas
Cohn J, Kinder B, Jamieson J, Delahunt N, Gorelick F. Purification and properties of a multifunctional calcium/calmodulin-dependent protein kinase from rat pancreas. Biochimica Et Biophysica Acta 1987, 928: 320-331. PMID: 3105599, DOI: 10.1016/0167-4889(87)90192-3.Peer-Reviewed Original ResearchConceptsCalmodulin protein kinaseCalcium/calmodulin-dependent protein kinaseCalmodulin-dependent protein kinaseProtein kinaseMultifunctional calcium/calmodulin-dependent protein kinaseTwo-dimensional gel electrophoresisRibosomal proteinsThreonine residuesLarge subunitCellular functionsRibosomal substratesSubstrate specificityKinaseProteolytic degradationSubunitsGel electrophoresisHydrophobic chromatographyAffinity chromatographyPolyacrylamide gelsCalmodulinPurification procedureGel filtrationEnzyme preparationAutophosphorylationTissue
1983
Calmodulin-stimulated protein kinase activity from rat pancreas.
Gorelick FS, Cohn JA, Freedman SD, Delahunt NG, Gershoni JM, Jamieson JD. Calmodulin-stimulated protein kinase activity from rat pancreas. Journal Of Cell Biology 1983, 97: 1294-1298. PMID: 6619194, PMCID: PMC2112629, DOI: 10.1083/jcb.97.4.1294.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCalcium-Binding ProteinsCalmodulinMolecular WeightPancreasPhosphorylationProtein KinasesRatsRibosomal Proteins