1992
Phosphorylation of elongation factor 2 during Ca2+-mediated secretion from rat parotid acini
Hincke M, Nairn A. Phosphorylation of elongation factor 2 during Ca2+-mediated secretion from rat parotid acini. Biochemical Journal 1992, 282: 877-882. PMID: 1372803, PMCID: PMC1130869, DOI: 10.1042/bj2820877.Peer-Reviewed Original ResearchConceptsElongation factor 2Protein synthesisFactor 2Two-dimensional PAGECalmodulin-dependent phosphorylationRapid phosphorylationParotid acinar cellsMolecular mechanismsRat parotid cellsPhosphorylationPhorbol esterStimulation of secretionProteinParotid cellsAcinar cellsRat parotid aciniParotid aciniSpecific antiseraCellsCa2ImmunoprecipitationExtracellular Ca2SecretionStimulationInhibition
1991
Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane
Thelen M, Rosen A, Nairn A, Aderem A. Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane. Nature 1991, 351: 320-322. PMID: 2034276, DOI: 10.1038/351320a0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAutoradiographyCell MembraneEnzyme ActivationEthers, CyclicHumansIntracellular Signaling Peptides and ProteinsKineticsMembrane ProteinsMyristic AcidMyristic AcidsMyristoylated Alanine-Rich C Kinase SubstrateNeutrophilsN-Formylmethionine Leucyl-PhenylalanineOkadaic AcidPhosphorus RadioisotopesPhosphorylationProtein Kinase CProteinsTritiumConceptsProtein kinase CProtein kinase C substrateAlanine-rich C kinase substrateActin-membrane interactionsMembrane-bound substratesActin-binding proteinsSpecific PKC substrateC kinase substrateReceptor-mediated signalsMembrane targetingKinase substrateMembrane attachmentPKC substratePlasma membraneSubsequent dephosphorylationKinase CC substrateMARCKSNovel mechanismReversible associationProteinMembraneEffective bindingMyristoylationMacrophage activation