Search results for "Lipoylation"

showing 6 items of 6 documents

Palmitoylation is a post-translational modification of Alix regulating the membrane organization of exosome-like small extracellular vesicles.

2018

Abstract Background Virtually all cell types have the capacity to secrete nanometer-sized extracellular vesicles, which have emerged in recent years as potent signal transducers and cell-cell communicators. The multifunctional protein Alix is a bona fide exosomal regulator and skeletal muscle cells can release Alix-positive nano-sized extracellular vesicles, offering a new paradigm for understanding how myofibers communicate within skeletal muscle and with other organs. S-palmitoylation is a reversible lipid post-translational modification, involved in different biological processes, such as the trafficking of membrane proteins, achievement of stable protein conformations, and stabilization…

0301 basic medicineAlix (also known as PDCD6IP)Protein ConformationLipoylationLipid BilayersBiophysicsSkeletal muscle cellsCell Cycle ProteinsExosomesBiochemistryExosomeTetraspanin 29Cell Line03 medical and health sciencesExtracellular VesiclesPalmitoylationTetraspaninExtracellularHumansLipid bilayerMuscle SkeletalMolecular BiologyCells CulturedEndosomal Sorting Complexes Required for TransportChemistryVesicleCalcium-Binding ProteinsCell MembraneExtracellular vesicleTetraspaninSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Cell biologyExosomeProtein Transport030104 developmental biologyS-palmitoylationMembrane proteinextracellular vesicles (EVs)Skeletal muscle cellProtein Processing Post-TranslationalProtein BindingSignal TransductionBiochimica et biophysica acta. General subjects
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Quantitative characterization of tetraspanin 8 homointeractions in the plasma membrane

2021

The spatial distribution of proteins in cell membranes is crucial for signal transduction, cell communication and membrane trafficking. Members of the Tetraspanin family organize functional protein clusters within the plasma membrane into so-called Tetraspanin-enriched microdomains (TEMs). Direct interactions between Tetraspanins are believed to be important for this organization. However, studies thus far have utilized mainly co-immunoprecipitation methods that cannot distinguish between direct and indirect, through common partners, interactions. Here we study Tetraspanin 8 homointeractions in living cells via quantitative fluorescence microscopy. We demonstrate that Tetraspanin 8 exists i…

Cell signalingTetraspaninsLipoylationDimerTransfectionBiochemistryArticleProtein–protein interactionchemistry.chemical_compoundMembrane MicrodomainsTetraspaninFluorescence Resonance Energy TransferHumansMolecular BiologyChemistryCell BiologyDissociation constantHEK293 CellsMembraneMicroscopy FluorescenceMembrane proteinembryonic structuresBiophysicsThermodynamicsProtein MultimerizationSignal transductionSignal TransductionBiochemical Journal
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Palmitoylation of Pulmonary Surfactant Protein SP-C Is Critical for Its Functional Cooperation with SP-B to Sustain Compression/Expansion Dynamics in…

2010

AbstractRecent data suggest that a functional cooperation between surfactant proteins SP-B and SP-C may be required to sustain a proper compression-expansion dynamics in the presence of physiological proportions of cholesterol. SP-C is a dually palmitoylated polypeptide of 4.2 kDa, but the role of acylation in SP-C activity is not completely understood. In this work we have compared the behavior of native palmitoylated SP-C and recombinant nonpalmitoylated versions of SP-C produced in bacteria to get a detailed insight into the importance of the palmitic chains to optimize interfacial performance of cholesterol-containing surfactant films. We found that palmitoylation of SP-C is not essenti…

LipoylationSus scrofaBiophysicsAcute respiratory distressModels Biologicallaw.inventionAcylationchemistry.chemical_compoundPalmitoylationPulmonary surfactantlawAnimalsPulmonary Surfactant-Associated Protein BChemistryCholesterolMembraneTemperaturePulmonary SurfactantsBiofísicaPulmonary Surfactant-Associated Protein CBiomechanical PhenomenaCholesterolBiochemistryBiophysicsRecombinant DNAlipids (amino acids peptides and proteins)AdsorptionProteïnes
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Loss of function mutation in the palmitoyl-transferase HHAT leads to syndromic 46,XY disorder of sex development by impeding Hedgehog protein palmito…

2014

The Hedgehog (Hh) family of secreted proteins act as morphogens to control embryonic patterning and development in a variety of organ systems. Post-translational covalent attachment of cholesterol and palmitate to Hh proteins are critical for multimerization and long range signaling potency. However, the biological impact of lipid modifications on Hh ligand distribution and signal reception in humans remains unclear. In the present study, we report a unique case of autosomal recessive syndromic 46,XY Disorder of Sex Development (DSD) with testicular dysgenesis and chondrodysplasia resulting from a homozygous G287V missense mutation in the hedgehog acyl-transferase (HHAT) gene. This mutation…

MaleCancer Research[SDV]Life Sciences [q-bio]medicine.disease_causeCell Fate DeterminationMiceTestisMorphogenesisMissense mutationddc:576.5Genetics (clinical)MutationHomozygoteCell DifferentiationHedgehog signaling pathwayPedigreeCell biologyFemaleSignal transductionSignal TransductionResearch Articlemedicine.medical_specialtylcsh:QH426-470LipoylationMolecular Sequence DataMutation MissenseBiologyPalmitoylationHHATInternal medicineGeneticsmedicineAnimalsHumansHedgehog ProteinsAmino Acid SequenceMolecular BiologyHedgehogEcology Evolution Behavior and SystematicsDisorder of Sex Development 46XY[ SDV ] Life Sciences [q-bio]Sequence Homology Amino AcidBiology and Life SciencesSex Determinationlcsh:GeneticsEndocrinology46 XY Disorders of Sex Development/*genetics; Acyltransferases/chemistry/*genetics/metabolism; Amino Acid Sequence; Animals; Female; Hedgehog Proteins/*metabolism; Homozygote; Humans; Lipoylation/*genetics; Male; Mice; Molecular Sequence Data; *Mutation Missense; Pedigree; Sequence Homology Amino Acid; Signal Transduction/*genetics; Testis/embryologyLipid modificationAcyltransferasesDevelopmental 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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The Extracellular δ-Domain is Essential for the Formation of CD81 Tetraspanin Webs

2014

AbstractCD81 is a ubiquitously expressed member of the tetraspanin family. It forms large molecular platforms, so-called tetraspanin webs that play physiological roles in a variety of cellular functions and are involved in viral and parasite infections. We have investigated which part of the CD81 molecule is required for the formation of domains in the cell membranes of T-cells and hepatocytes. Surprisingly, we find that large CD81 platforms assemble via the short extracellular δ-domain, independent from a strong primary partner binding and from weak interactions mediated by palmitoylation. The δ-domain is also essential for the platforms to function during viral entry. We propose that, ins…

virusesLipoylationBiophysicschemical and pharmacologic phenomenaPlasma protein bindingBiologyTetraspanin 28Jurkat CellsProtein structurePalmitoylationTetraspaninViral entryExtracellularHumansComputingMilieux_MISCELLANEOUS[PHYS]Physics [physics]MembranesHep G2 Cellsbiochemical phenomena metabolism and nutritionCell biologyProtein Structure TertiaryProtein MultimerizationProtein Processing Post-TranslationalFunction (biology)CD81Protein Binding
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