2003
Calcium/calmodulin dependent protein kinase II constitutively binds and regulates the ileal BB Na+/H+ exchanger NHE3
Zizak M, Bartonicek D, Cha B, Murtazina R, Kim J, Lee-Kwon W, Gorelick F, Tse M, Donowitz M. Calcium/calmodulin dependent protein kinase II constitutively binds and regulates the ileal BB Na+/H+ exchanger NHE3. Gastroenterology 2003, 124: a471. DOI: 10.1016/s0016-5085(03)82384-3.Peer-Reviewed Original Research
1995
Ca2+/calmodulin-dependent protein kinase II activation and regulation of adrenal glomerulosa Ca2+ signaling
Fern RJ, Hahm MS, Lu HK, Liu LP, Gorelick FS, Barrett PQ. Ca2+/calmodulin-dependent protein kinase II activation and regulation of adrenal glomerulosa Ca2+ signaling. American Journal Of Physiology 1995, 269: f751-f760. PMID: 8594869, DOI: 10.1152/ajprenal.1995.269.6.f751.Peer-Reviewed Original ResearchConceptsCaMKII activityBovine adrenal glomerulosa cellsDepolarization-induced increaseAdrenal glomerulosa cellsDepolarization-induced Ca2Voltage-gated Ca2Independent CaMKII activityElevated extracellular potassiumDependent protein kinase II (CaMKII) activationCaMKII inhibitor peptideAgonist-induced stimulationAldosterone secretagoguesAngiotensin IIGlomerulosa cellsKinase activityExtracellular potassiumImportance of CaMKIIIntracellular Ca2Dependent protein kinase IIProtein kinase IICell treatmentKN-62Calmodulin antagonistsCell-permeable inhibitorChannel activity
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
Distribution 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
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
1988
Autophosphorylation 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-XaaDevelopment of Secretagogue Responsiveness in the Pancreas
Jamieson JD, Gorelick FS, Chang A. Development of Secretagogue Responsiveness in the Pancreas. Scandinavian Journal Of Gastroenterology 1988, 23: 98-103. PMID: 2852401, DOI: 10.3109/00365528809095920.Peer-Reviewed Original ResearchConceptsSecretory pathwaySecretory proteinsPancreatic acinar cellsEpithelial cell polarityDependent protein kinase IIRegulated secretory pathwayConstitutive secretory pathwayAcinar cellsProtein kinase IICell polarityMembrane proteinsPhosphorylated substratesRegulated secretionBasolateral domainCell biologyPlasmalemmal domainsPlasma membraneKinase IISecond messengerSecretagogue responsivenessFunctional specializationProteinEpithelial cellsPathwayZymogen granules