Search results for "cytoskeleton"

showing 10 items of 272 documents

The long-term cytoskeletal rearrangement induced by rabbit enteropathogenic Escherichia coli is Esp dependent but intimin independent.

1999

Attaching and effacing rabbit enteropathogenic Escherichia coli (REPEC) of the O103 serogroup adhere diffusely on HeLa cells and trigger a slow progressive cytopathic effect (CPE) characterized by the recruitment of vinculin and the assembly of actin stress fibres. In contrast to REPEC O103, the reference human EPEC strain E2348/69 is unable to trigger the CPE. In this study, we have shown first that the fimbrial adhesin AF/R2, which mediates the diffuse adhesion of REPEC O103, was not sufficient to induce the CPE capability upon E2348/69. Non-polar mutants of REPEC O103 for espA, espB, espD and eae were then constructed. The four mutants were unable to induce attaching and effacing lesions…

DNA BacterialMutantMolecular Sequence DataMicrobiologyBacterial AdhesionMicrobiology03 medical and health sciencesBacterial ProteinsEscherichia coliAnimalsHumansEnteropathogenic Escherichia coliCytoskeletonAdhesins BacterialMolecular Biology[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyActinCytoskeleton030304 developmental biologyIntiminCytopathic effect0303 health sciencesAdhesins Escherichia colibiologyBase Sequence030306 microbiologyEscherichia coli ProteinsGenetic Complementation TestREARRANGEMENTbiochemical phenomena metabolism and nutritionVinculinBacterial adhesin[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyGenes Bacterialbiology.proteinRabbitsCarrier ProteinsBacterial Outer Membrane ProteinsHeLa CellsMolecular microbiology
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Myosin VIIa, harmonin and cadherin 23, three Usher I gene products that cooperate to shape the sensory hair cell bundle

2002

Deaf-blindness in three distinct genetic forms of Usher type I syndrome (USH1) is caused by defects in myosin VIIa, harmonin and cadherin 23. Despite being critical for hearing, the functions of these proteins in the inner ear remain elusive. Here we show that harmonin, a PDZ domain-containing protein, and cadherin 23 are both present in the growing stereocilia and that they bind to each other. Moreover, we demonstrate that harmonin b is an F-actin-bundling protein, which is thus likely to anchor cadherin 23 to the stereocilia microfilaments, thereby identifying a novel anchorage mode of the cadherins to the actin cytoskeleton. Moreover, harmonin b interacts directly with myosin VIIa, and i…

DNA ComplementaryCadherin Related ProteinsCell Cycle Proteinsmacromolecular substancesMyosinsBiologyTransfectionMicrofilamentGeneral Biochemistry Genetics and Molecular BiologyCell LineMiceCDH23Two-Hybrid System TechniquesHair Cells Auditoryotorhinolaryngologic diseasesmedicineAnimalsHumansProtein IsoformsRats WistarMolecular BiologyActinAdaptor Proteins Signal TransducingGene LibraryGeneral Immunology and MicrobiologyCadherinGeneral NeuroscienceStereociliaDyneinsCell DifferentiationArticlesCadherinsActin cytoskeletonActinsProtein Structure TertiaryRatsCell biologyCytoskeletal ProteinsMicroscopy Electronmedicine.anatomical_structureMicroscopy FluorescenceMyosin VIIasense organsCarrier ProteinsTip linkPCDH15HeLa CellsProtein BindingThe EMBO Journal
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The glycosyltransferase activities of lysyl hydroxylase 3 (LH3) in the extracellular space are important for cell growth and viability.

2008

Abstract Lysyl hydroxylase (LH) isoform 3 is a post-translational enzyme possessing LH, collagen galactosyltransferase (GT) and glucosyltransferase (GGT) activities. We have demonstrated that LH3 is found not only intracellularly, but also on the cell surface and in the extracellular space, suggesting additional functions for LH3. Here we show that the targeted disruption of LH3 by siRNA causes a marked reduction of both glycosyltransferase activities, and the overexpression of LH3 in HT-1080 cells increases hydroxylation of lysyl residues and the subsequent galactosylation and glucosylation of hydroxylysyl residues. These data confirm the multi-functionality of LH3 in cells. Furthermore, t…

DNA ComplementaryGlycosylationCell SurvivalLysyl hydroxylaseCellhydroxylysyl glycosylationFluorescent Antibody Techniquelysyl hydroxylaseMicrotubulesPermeabilityCell LineGlycosyltransferasemedicineExtracellularAnimalsHumanscell growthViability assayRNA Small InterferingCell Shapecell viabilityCell ProliferationbiologyCell DeathCell growthProcollagen-Lysine 2-Oxoglutarate 5-Dioxygenasecollagen biosynthesisGlycosyltransferasesCell BiologyArticlesGalactosyltransferasesMolecular biologyPeptide FragmentsCulture MediaActin Cytoskeletonmedicine.anatomical_structurepost-translational modificationCell culturebiology.proteinMolecular MedicineGlucosyltransferaseExtracellular Spacehydroxylysyl glycosyltransferaseJournal of cellular and molecular medicine
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Identification of protein IT of the intestinal cytoskeleton as a novel type I cytokeratin with unusual properties and expression patterns.

1990

A major cytoskeletal polypeptide (Mr approximately 46,000; protein IT) of human intestinal epithelium was characterized by biochemical and immunological methods. The polypeptide, which was identified as a specific and genuine mRNA product by translation in vitro, reacted, in immunoblotting after SDS-PAGE, only with one of numerous cytokeratin (CK) antisera tested but with none of many monoclonal CK antibodies. In vitro, it formed heterotypic complexes with the type II CK 8, as shown by blot binding assays and gel electrophoresis in 4 M urea, and these complexes assembled into intermediate filaments (IFs) under appropriate conditions. A chymotrypsin-resistant Mr approximately 38,000 core fra…

DuodenumImmunoblottingMolecular Sequence DataBiologyPeptide MappingEpitheliumCytokeratinIntestinal mucosaSequence Homology Nucleic AcidKeratinProtein biosynthesisAnimalsHumansElectrophoresis Gel Two-DimensionalAmino Acid SequenceRNA MessengerIntestinal MucosaIntermediate filamentCytoskeletonPeptide sequenceCytoskeletonchemistry.chemical_classificationArticlesCell BiologyMolecular biologyRatsBlotCytoskeletal ProteinsMicroscopy ElectronBiochemistrychemistryProtein BiosynthesisKeratinsJournal of Cell Biology
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Atomic Structures of Two Novel Immunoglobulin-like Domain Pairs in the Actin Cross-linking Protein Filamin

2009

Filamins are actin filament cross-linking proteins composed of an N-terminal actin-binding domain and 24 immunoglobulin-like domains (IgFLNs). Filamins interact with numerous proteins, including the cytoplasmic domains of plasma membrane signaling and cell adhesion receptors. Thereby filamins mechanically and functionally link the cell membrane to the cytoskeleton. Most of the interactions have been mapped to the C-terminal IgFLNs 16–24. Similarly, as with the previously known compact domain pair of IgFLNa20–21, the two-domain fragments IgFLNa16–17 and IgFLNa18–19 were more compact in small angle x-ray scattering analysis than would be expected for two independent domains. Solution state NM…

EGF-like domainFilaminsMolecular Sequence DataMolecular ConformationImmunoglobulinsmacromolecular substancesPlasma protein bindingBiologyFilaminModels BiologicalBiochemistryCell membraneHAMP domain03 medical and health sciencesContractile Proteins0302 clinical medicineddc:570Cell AdhesionmedicineHumansScattering RadiationAmino Acid SequenceCytoskeletonCell adhesionMolecular BiologyCytoskeletonActin030304 developmental biology0303 health sciencesMicrofilament ProteinsCell BiologyActinsRecombinant ProteinsProtein Structure Tertiary3. Good healthCell biologyCross-Linking Reagentsmedicine.anatomical_structureProtein Structure and Folding030217 neurology & neurosurgeryProtein BindingJournal of Biological Chemistry
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Long-lasting exocytosis and massive structural reorganisation in the egg periphery during cortical reaction inPlatynereis dumerilii(Annelida, Polycha…

1995

SummaryThe course of the cortical reaction in thePlatynereis dumeriliiegg is described from live observation and from sectioned fixed material and is found to differ in several aspects from the course of cortical reactions in better-known systems. Cortical granules are unusually numerous. They are discharged by exocytosis during a period of about 25 min following fertilisation (18°C). Most of the surplus membrane material brought to the egg surface by exocytosis is set free into the perivitelline space. Swelling of egg jelly precursor secreted by cortical granule exocytosis may be causal for the detachment of the vitelline envelope from the egg cell surface which, however, remains attached …

Egg cellCytochalasin DVitelline membranePerivitelline spaceExocytosismedicineAnimalsCytoskeletonCell SizeOvumMicrovillibiologyChemistryCortical granule exocytosisNocodazoleCell MembranePolychaetaCell Biologybiology.organism_classificationOocyteCell biologyMicroscopy Electronmedicine.anatomical_structureMicroscopy FluorescenceFertilizationCortical reactionEgg jellyDevelopmental BiologyPlatynereisZygote
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The p21-activated kinase Mbt is a component of the apical protein complex in central brain neuroblasts and controls cell proliferation

2013

The final size of the central nervous system is determined by precisely controlled generation, proliferation and death of neural stem cells. We show here that the Drosophila PAK protein Mushroom bodies tiny (Mbt) is expressed in central brain progenitor cells (neuroblasts) and becomes enriched to the apical cortex of neuroblasts in a cell cycle- and Cdc42-dependent manner. Using mushroom body neuroblasts as a model system, we demonstrate that in the absence of Mbt function, neuroblasts and their progeny are correctly specified and are able to generate different neuron subclasses as in the wild type, but are impaired in their proliferation activity throughout development. In general, loss of…

Embryo Nonmammaliananimal structuresMitosisApoptosisCell CountSpindle ApparatusBiologyNeural Stem CellsNeuroblastGTP-Binding ProteinsTubulinCell polarityAnimalsDrosophila ProteinsProgenitor cellMolecular BiologyMitosisCell ProliferationCell SizeBinding SitesApical cortexAsymmetric Cell DivisionfungiBrainCell PolarityGene Expression Regulation DevelopmentalNeural stem cellCell biologyEnzyme ActivationActin CytoskeletonPhenotypenervous systemLarvaMultiprotein Complexesembryonic structuresMushroom bodiesDrosophilaProtein KinasesGanglion mother cellDevelopmental BiologyDevelopment
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Improvement in Nuclear Entry and Transgene Expression of Baculoviruses by Disintegration of Microtubules in Human Hepatocytes

2005

ABSTRACT Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV), a potent virus for mammalian cell gene delivery, possesses an ability to transduce mammalian cells without viral replication. We examined the role of the cellular cytoskeleton in the cytoplasmic trafficking of viral particles toward the nucleus in human hepatic cells. Microscopic studies showed that capsids were found in the nucleus after either viral inoculation or cytoplasmic microinjection of nucleocapsids. The presence of microtubule (MT) depolymerizing agents caused the amount of nuclear capsids to increase. Overexpression of p50/dynamitin, an inhibitor of dynein-dependent endocytic trafficking from peripheral e…

EndosomeMicrotubule-associated proteinvirusesImmunologyEndocytic cycleGenetic VectorsActive Transport Cell NucleusGene ExpressionBiologyGene deliveryMicrobiologyMicrotubulesCell Linechemistry.chemical_compoundTransduction GeneticVirologyHumansNucleocapsidCytoskeletonDynactin Complexbeta-GalactosidaseMolecular biologyNucleopolyhedrovirusesRecombinant ProteinsVirus-Cell InteractionsNocodazoleMicroscopy ElectronViral replicationchemistryLac OperonCell cultureCytoplasmInsect ScienceHepatocytesMicrotubule-Associated Proteins
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Small heat shock proteins and the cytoskeleton: an essential interplay for cell integrity?

2012

Abstract The cytoskeleton is a highly complex network of three major intracellular filaments, microfilaments (MFs), microtubules (MTs) and intermediate filaments (IFs). This network plays a key role in the control of cell shape, division, functions and interactions in animal organs and tissues. Dysregulation of the network can contribute to numerous human diseases. Although small HSPs (sHSPs) and in particular HSP27 (HSPB1) or αB-crystallin (HSPB5) display a wide range of cellular properties, they are mostly known for their ability to protect cells under stress conditions. Mutations in some sHSPs have been found to affect their ability to interact with cytoskeleton proteins, leading to IF a…

Epithelial-Mesenchymal TransitionIntermediate FilamentsVimentinmacromolecular substancesMicrofilamentBiochemistry03 medical and health sciences0302 clinical medicineHsp27MicrotubuleStress PhysiologicalHeat shock proteinNeoplasmsAnimalsHumansCytoskeletonIntermediate filament030304 developmental biology0303 health sciencesbiologyGenetic Diseases InbornCell BiologyFibrosisCell biologyHeat-Shock Proteins SmallMutationbiology.proteinDesmin030217 neurology & neurosurgeryThe international journal of biochemistrycell biology
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Immunodetection of the microvillous cytoskeleton molecules villin and ezrin in the parasitophorous vacuole wall of Cryptosporidium parvum (Protozoa: …

1999

Microvilli - actin - villin - ezrin - Cryptosporidium parvum The sporozoites and merozoites of the Apicomplexan protozoan Cryptosporidium parvum (C. parvum) invade the apical side of enterocytes and induce the formation of a parasitophorous vacuole which stays in the brush border area and disturbs the distribution of microvilli. The vacuole is separated from the apical cytoplasm of the cell by an electron-dense layer of undetermined composition. In order to characterize the enterocyte cytoskeleton changes that occur during C. parvum invasion and development, we used both confocal immunofluorescence and immunoelectron microscopy to examine at the C.parvum-enterocyte interface the distributio…

Feces/microbiologyIntestines/parasitologyMicrofilament Proteins/ analysisVacuoleddc:616.07Actins/analysisRats Sprague-DawleyFecesMiceEzrinCarrier Proteins/ analysisCryptosporidium/ chemistry/pathogenicity/ultrastructureCytoskeletonMicroscopy ImmunoelectronCytoskeletonMice Inbred BALB CMicroscopy ConfocalbiologyMicrovilliMicrofilament ProteinsCytoskeleton/ chemistryGeneral MedicineCell biologyIntestinesCryptosporidium parvumFemaleVillinHistologyImmunoelectron microscopyVacuoles/ultrastructurePhosphoproteins/ analysisCryptosporidiummacromolecular substancesPathology and Forensic Medicineparasitic diseasesAnimalsApical cytoplasmActinCell Biologybiology.organism_classificationPhosphoproteinsActinsRatsMicrovilli/ chemistryCytoskeletal ProteinsMicroscopy ElectronVacuolesbiology.proteinCarrier ProteinsEuropean journal of cell biology
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