Search results for "Myristoylation"

showing 5 items of 5 documents

Interaction of Neuronal Calcium Sensor-1 (NCS-1) with Phosphatidylinositol 4-Kinase β Stimulates Lipid Kinase Activity and Affects Membrane Trafficki…

2001

Phosphatidylinositol 4-kinases (PI4K) catalyze the first step in the synthesis of phosphatidylinositol 4,5-bisphosphate, an important lipid regulator of several cellular functions. Here we show that the Ca(2+)-binding protein, neuronal calcium sensor-1 (NCS-1), can physically associate with the type III PI4Kbeta with functional consequences affecting the kinase. Recombinant PI4Kbeta, but not its glutathione S-transferase-fused form, showed enhanced PI kinase activity when incubated with recombinant NCS-1, but only if the latter was myristoylated. Similarly, in vitro translated NCS-1, but not its myristoylation-defective mutant, was found associated with recombinant- or in vitro translated P…

Cell Membrane PermeabilityLipoproteinsNeuronal Calcium-Sensor ProteinsLipid kinase activityBiologyPhosphatidylinositolsbehavioral disciplines and activitiesBiochemistrychemistry.chemical_compoundsymbols.namesakePhosphatidylinositol PhosphatesChlorocebus aethiopsmental disordersAnimalsCalcium SignalingPhosphatidylinositol1-Phosphatidylinositol 4-KinaseMolecular BiologyCellular compartmentMyristoylationKinaseCalcium-Binding ProteinsCell MembraneNeuropeptidesBiological TransportCell BiologyTransfectionGolgi apparatusCell CompartmentationRatsCell biologychemistryBiochemistryNeuronal calcium sensor-1COS Cellssymbolsbiology.proteinCattleMyristic AcidsProtein Processing Post-TranslationalProtein BindingJournal of Biological Chemistry
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Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein 1 1Edited by A. R. Fersht

1999

Negative factor (Nef) is a regulatory myristoylated protein of human immunodeficiency virus (HIV) that has a two-domain structure consisting of an anchor domain and a core domain separated by a specific cleavage site of the HIV proteases. For structural analysis, the HIV-1 Nef anchor domain (residues 2-57) was synthesized with a myristoylated and non-myristoylated N terminus. The structures of the two peptides were studied by1H NMR spectroscopy and a structural model was obtained by restrained molecular dynamic simulations. The non-myristoylated peptide does not have a unique, compactly folded structure but occurs in a relatively extended conformation. The only rather well-defined canonical…

ChemistryViral proteinStereochemistrySequence alignmentmedicine.disease_causeSerineCrystallographyProtein structureStructural BiologyHelixmedicinelipids (amino acids peptides and proteins)Molecular BiologyProtein secondary structurePeptide sequenceMyristoylationJournal of Molecular Biology
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A Membrane-Bound Vertebrate Globin

2011

The family of vertebrate globins includes hemoglobin, myoglobin, and other O(2)-binding proteins of yet unclear functions. Among these, globin X is restricted to fish and amphibians. Zebrafish (Danio rerio) globin X is expressed at low levels in neurons of the central nervous system and appears to be associated with the sensory system. The protein harbors a unique N-terminal extension with putative N-myristoylation and S-palmitoylation sites, suggesting membrane-association. Intracellular localization and transport of globin X was studied in 3T3 cells employing green fluorescence protein fusion constructs. Both myristoylation and palmitoylation sites are required for correct targeting and m…

Protein StructureLipoylationGreen Fluorescent ProteinsMolecular Sequence Datalcsh:MedicineHemeBiochemistryCell membranechemistry.chemical_compoundModel OrganismsPalmitoylationhemic and lymphatic diseasesmedicineAnimalsRespiratory functionAmino Acid SequenceGlobinlcsh:ScienceProtein InteractionsBiologyZebrafishZebrafishMyristoylationHemoproteinsMultidisciplinarySequence Homology Amino Acidbiologylcsh:RCell MembraneMembrane ProteinsProteinsGene Expression Regulation DevelopmentalAnimal Modelsbiology.organism_classificationRecombinant ProteinsGlobinsGlobin foldOxygenmedicine.anatomical_structureBiochemistryMyoglobinchemistryImmunoglobulin GCytochemistrylcsh:QRabbitsResearch ArticleSubcellular FractionsPLoS ONE
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Dimerization of visinin-like protein 1 is regulated by oxidative stress and calcium and is a pathological hallmark of amyotrophic lateral sclerosis

2014

AbstractRedox control of proteins that form disulfide bonds upon oxidative challenge is an emerging topic in the physiological and pathophysiological regulation of protein function. We have investigated the role of the neuronal calcium sensor protein visinin-like protein 1 (VILIP-1) as a novel redox sensor in a cellular system. We have found oxidative stress to trigger dimerization of VILIP-1 within a cellular environment and identified thioredoxin reductase as responsible for facilitating the remonomerization of the dimeric protein. Dimerization is modulated by calcium and not dependent on the myristoylation of VILIP-1. Furthermore, we show by site-directed mutagenesis that dimerization is…

Thioredoxin reductaseAmino Acid MotifsBlotting Westernchemistry.chemical_elementMice TransgenicFree radicalsOxidative phosphorylationCalciumProtein aggregationmedicine.disease_causeBiochemistryMass SpectrometryMicechemistry.chemical_compoundSuperoxide Dismutase-1BAPTAPhysiology (medical)VILIP-1medicineAnimalsHumansCysteineMyristoylationSuperoxide DismutaseChemistryHEK 293 cellsAmyotrophic lateral sclerosisRedox sensorImmunohistochemistryCell biologyDisease Models AnimalOxidative StressHEK293 CellsBiochemistryNeurocalcinMutagenesis Site-DirectedCalciumProtein MultimerizationOxidation-ReductionOxidative stressFree Radical Biology and Medicine
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The Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) is Sequentially Phosphorylated by Conventional, Novel and Atypical Isotypes of Protein Kin…

1995

The myristoylated alanine-rich C-kinase substrate (MARCKS) is the major protein kinase C (PKC) substrate in many cell types including fibroblasts and brain cells. Here we describe the phosphorylation of MARCKS and the site specificity for different PKC isotypes. Conventional (c)PKC beta 1, novel (n)PKC delta and nPKC epsilon efficiently phosphorylated the MARCKS protein in vitro. The Km values were extremely low, reflecting a high affinity between kinases and substrate. The apparent affinity of nPKC delta (Km = 0.06 microM) was higher than that of nPKC epsilon and cPKC beta 1 (Km = 0.32 microM). The rate of substrate phosphorylation was inversely correlated with affinity and decreased in th…

inorganic chemicalsKinaseChemistryIntracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsContext (language use)macromolecular substancesenvironment and public healthBiochemistryMolecular biologyCell biologyIsoenzymesSerineKineticsenzymes and coenzymes (carbohydrates)Substrate-level phosphorylationbacteriaPhosphorylationPhosphorylationMARCKSMyristoylated Alanine-Rich C Kinase SubstrateProtein Kinase CProtein kinase CMyristoylationEuropean Journal of Biochemistry
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