2001
Synapsin I is expressed in epithelial cells: localization to a unique trans-Golgi compartment.
Bustos R, Kolen E, Braiterman L, Baines A, Gorelick F, Hubbard A. Synapsin I is expressed in epithelial cells: localization to a unique trans-Golgi compartment. Journal Of Cell Science 2001, 114: 3695-704. PMID: 11707521, DOI: 10.1242/jcs.114.20.3695.Peer-Reviewed Original ResearchConceptsSynapsin ITrans-Golgi compartmentSynaptic vesicle exocytosisProtein kinase ANon-neuronal cell linesBrain synapsin IEpithelial cellsNorthern blot analysisTrafficking pathwaysVesicle exocytosisVesicular compartmentsKinase AMyosin IIGolgi complexLimited proteolysisAnti-synapsin antibodiesPre-synaptic terminalsPeptide mapsBlot analysisCell linesCompartmentsCellsNeural tissueLiver cellsCytoskeleton
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
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
1990
Rabbit ileal villus cell brush border Na+/H+ exchange is regulated by Ca2+/calmodulin-dependent protein kinase II, a brush border membrane protein.
Cohen ME, Reinlib L, Watson AJ, Gorelick F, Rys-Sikora K, Tse M, Rood RP, Czernik AJ, Sharp GW, Donowitz M. Rabbit ileal villus cell brush border Na+/H+ exchange is regulated by Ca2+/calmodulin-dependent protein kinase II, a brush border membrane protein. Proceedings Of The National Academy Of Sciences Of The United States Of America 1990, 87: 8990-8994. PMID: 2174171, PMCID: PMC55086, DOI: 10.1073/pnas.87.22.8990.Peer-Reviewed Original ResearchConceptsDependent protein kinase IIProtein kinase IIKinase IIMembrane proteinsSynapsin IDependent protein kinase activityDependent protein kinaseBrush border membranePhosphorylation of sitesProtein kinase activityInhibitor peptideCaM kinase IIBrush border membrane proteinsBorder membraneSpecific inhibitor peptidePhosphopeptide mappingBrush borderProtein kinaseMicrovillus membrane proteinsKinase activityIleal brush-border membraneVillus cell brush border membraneApical membraneKinaseVesicle preparations
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 fractionPresence of calcium/calmodulin‐dependent protein Kinase II in Nerve terminals of rat brain
Walaas S, Gorelick F, Greengard P. Presence of calcium/calmodulin‐dependent protein Kinase II in Nerve terminals of rat brain. Synapse 1989, 3: 356-362. PMID: 2545012, DOI: 10.1002/syn.890030409.Peer-Reviewed Original ResearchConceptsCalcium/calmodulin-dependent protein kinase IICalmodulin-dependent protein kinase IISubstantia nigraProtein kinase IINerve terminalsRat brainSynapsin INerve terminal markersLesion-induced degenerationLesion-induced changesCalcium/calmodulin-dependent protein kinase type IIPrevious immunocytochemical studiesKinase IIStriatonigral tractCorticostriatal tractPresynaptic terminalsNeuronal populationsCalmodulin-dependent protein kinase type IIMammalian brainCell bodiesImmunocytochemical studyTerminal markersBrainNeostriatumLesions
1987
Calcium-calmodulin-stimulated protein kinase in developing pancreas
Gorelick FS, Chang A, Jamieson JD. Calcium-calmodulin-stimulated protein kinase in developing pancreas. American Journal Of Physiology 1987, 253: g469-g476. PMID: 3116856, DOI: 10.1152/ajpgi.1987.253.4.g469.Peer-Reviewed Original ResearchConceptsCalmodulin-dependent protein kinaseProtein kinase activityCDPK activityProtein kinaseKinase activityEndogenous proteinsType II calmodulin-dependent protein kinaseType II Ca2Adult pancreasCaM-binding proteinsRelative molecular weightEmbryonic pancreasPancreatic developmentPancreatic acinar cellsGel filtration chromatographySecretagogue responsivenessCalcium-calmodulinExogenous substratesKinaseSynapsin IPancreatic maturationProteinPancreatic supernatantPhosphorylationSecretory process