Search results for "CELL POLARITY"

showing 10 items of 65 documents

The expression level of the orphan nuclear receptor GCNF (germ cell nuclear factor) is critical for neuronal differentiation.

2004

The germ cell nuclear factor (GCNF) is essential for normal embryonic development and gametogenesis. To test the prediction that GCNF is additionally required for neuronal differentiation, we used the mouse embryonal carcinoma cell line PCC7-Mz1, which represents an advantageous model to study neuronal cells from the stage of fate choice until the acquirement of functional competence. We generated stable transfectants that express gcnf sense or antisense RNA under the control of a tetracycline-regulated promoter. After retinoic acid-induced withdrawal from the cell cycle, sense clones developed a neuron network with changed properties, and the time course of neuron maturation was shortened.…

Patch-Clamp TechniquesGerm cell nuclear factorSynaptophysinDown-RegulationGene ExpressionReceptors Cytoplasmic and NuclearNerve Tissue ProteinsTretinoinBiologyNestinMiceEndocrinologyGAP-43 ProteinIntermediate Filament ProteinsNuclear Receptor Subfamily 6 Group A Member 1AnimalsRNA AntisenseMolecular BiologyNeuronsCell CycleCell PolarityCell DifferentiationGeneral MedicineCell cycleNestinCell biologyUp-RegulationNeuroepithelial cellDNA-Binding Proteinsnervous systemNeuron maturationSynaptophysinbiology.proteinNeuron differentiationStem cellMicrotubule-Associated ProteinsMolecular endocrinology (Baltimore, Md.)
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TALPID3 controls centrosome and cell polarity and the human ortholog KIAA0586 is mutated in Joubert syndrome (JBTS23)

2015

Joubert syndrome (JBTS) is a severe recessive neurodevelopmental ciliopathy which can affect several organ systems. Mutations in known JBTS genes account for approximately half of the cases. By homozygosity mapping and whole-exome sequencing, we identified a novel locus, JBTS23, with a homozygous splice site mutation in KIAA0586 (alias TALPID3), a known lethal ciliopathy locus in model organisms. Truncating KIAA0586 mutations were identified in two additional patients with JBTS. One mutation, c.428delG (p.Arg143Lysfs*4), is unexpectedly common in the general population and may be a major contributor to JBTS. We demonstrate KIAA0586 protein localization at the basal body in human and mouse p…

QH301-705.5chickenSciencePopulationCell Cycle ProteinsBiologymedicine.disease_causeRetinaGeneral Biochemistry Genetics and Molecular BiologyJoubert syndromeMiceTalpid3CerebellumJoubert syndromeCiliogenesismedicineAnimalsHumansBasal bodyAbnormalities MultiplehumanEye AbnormalitiesBiology (General)Human Biology and MedicineeducationmouseGeneticsMutationeducation.field_of_studyGeneral Immunology and MicrobiologyGeneral NeuroscienceCiliumQRGeneral MedicineKidney Diseases Cysticmedicine.diseaseKIAA05863. Good healthDisease Models Animalcell polarityCiliopathyDevelopmental Biology and Stem CellsciliopathycentrosomeCentrosomeMutationMedicineResearch ArticleeLife
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Critical Regulation of Early Th17 Cell Differentiation by Interleukin-1 Signaling

2009

SummaryT helper (Th) 17 cells have been recently discovered in both mouse and human. Here we show that interleukin-1 (IL-1) signaling on T cells is critically required for the early programming of Th17 cell lineage and Th17 cell-mediated autoimmunity. IL-1 receptor1 expression in T cells, which was induced by IL-6, was necessary for the induction of experimental autoimmune encephalomyelitis and for early Th17 cell differentiation in vivo. Moreover, IL-1 signaling in T cells was required in dendritic cell-mediated Th17 cell differentiation from naive or regulatory precursors and IL-1 synergized with IL-6 and IL-23 to regulate Th17 cell differentiation and maintain cytokine expression in effe…

Regulation of gene expressionEffectorCellular differentiationExperimental autoimmune encephalomyelitisImmunologychemical and pharmacologic phenomenahemic and immune systemsBiologymedicine.diseaseMolecular biologyCell biologyInfectious DiseasesCELLIMMUNOCell polaritymedicineImmunology and AllergyInterleukin 17Signal transductionMOLIMMUNOTranscription factorImmunity
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The human protein Hugl-1 substitutes for Drosophila lethal giant larvae tumour suppressor function in vivo

2004

Drosophila lethal giant larvae: (lgl), discs large (dlg) and scribble (scrib) are tumour suppressor genes acting in a common pathway, whose loss of function leads to disruption of cell polarity and tissue architecture, uncontrolled proliferation and growth of neoplastic lesions. Mammalian homologues of these genes are highly conserved and evidence is emerging concerning their role in cell proliferation control and tumorigenesis in humans. Here we investigate the functional conservation between Drosophila lethal giant larvae and its human homologue Hugl-1(Llgl1). We first show that Hugl-1 is lost in human solid malignancies, supporting its role as a tumour suppressor in humans. Hugl-1 expres…

SCRIBCancer ResearchTumor suppressor geneBiologymedicine.disease_causeEyelaw.inventionlawDrosophilidaeCell polarityGeneticsmedicineAnimalsDrosophila ProteinsHumansRNA MessengerMolecular BiologyGeneticsCell growthTumor Suppressor ProteinsfungiCell polarity; Drosophila; Epithelial cancers; Hugl-1; Lethal giant larvae; Tumour suppressorGene Expression Regulation DevelopmentalMembrane ProteinsProteinsHugl-1Lethal giant larvaebiology.organism_classificationCell biologyCytoskeletal ProteinsLarvaCell polaritySuppressorDrosophilaDrosophila melanogasterEpithelial cancersCarcinogenesisTumour suppressorProtein Binding
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PARD3 Inactivation in Lung Squamous Cell Carcinomas Impairs STAT3 and Promotes Malignant Invasion.

2015

Abstract Correct apicobasal polarization and intercellular adhesions are essential for the appropriate development of normal epithelia. Here, we investigated the contribution of the cell polarity regulator PARD3 to the development of lung squamous cell carcinomas (LSCC). Tumor-specific PARD3 alterations were found in 8% of LSCCs examined, placing PARD3 among the most common tumor suppressor genes in this malignancy. Most PAR3-mutant proteins exhibited a relative reduction in the ability to mediate formation of tight junctions and actin-based protrusions, bind atypical protein kinase C, activate RAC1, and activate STAT3 at cell confluence. Thus, PARD3 alterations prevented the formation of c…

STAT3 Transcription Factorrac1 GTP-Binding ProteinCancer ResearchLung NeoplasmsCellMice NudeRAC1Cell Cycle ProteinsBiologyArticleCell MovementCell Line TumorCell polaritymedicineAnimalsHumansNeoplasm InvasivenessProtein Kinase CAdaptor Proteins Signal TransducingCell ProliferationConfluencyTight junctionBase SequenceCell growthLiver NeoplasmsMembrane ProteinsSequence Analysis DNACell biologymedicine.anatomical_structureOncologyCell cultureMutationCancer researchCarcinoma Squamous CellTranscriptomeIntracellularNeoplasm TransplantationCancer research
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Rot1 plays an antagonistic role to Clb2 in actin cytoskeleton dynamics throughout the cell cycle.

2007

ROT1 is an essential gene whose inactivation causes defects in cell cycle progression and morphogenesis in budding yeast. Rot1 affects the actin cytoskeleton during the cell cycle at two levels. First, it is required for the maintenance of apical growth during bud growth. Second, Rot1 is necessary to polarize actin cytoskeleton to the neck region at the end of mitosis; because of this defect, rot1 cells do not properly form a septum to complete cell division. The inability to polarize the actin cytoskeleton at the end of mitosis is not due to a defect in the recruitment of the polarisome scaffold protein Spa2 or the actin cytoskeleton regulators Cdc42 and Cdc24 in the neck region. Previous …

Saccharomyces cerevisiae ProteinsGenes FungalArp2/3 complexmacromolecular substancesSaccharomyces cerevisiaeCyclin BActin remodeling of neuronsGene Expression Regulation FungalCDC2-CDC28 KinasesCytoskeletonCytoskeletonPolarisomebiologyCell CycleActin remodelingCell PolarityMembrane ProteinsCell BiologyActin cytoskeletonActinsCell biologyProfilinParacytophagyMutationbiology.proteinMolecular ChaperonesJournal of cell science
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MPP1 links the Usher protein network and the Crumbs protein complex in the retina.

2007

Contains fulltext : 53571.pdf (Publisher’s version ) (Closed access) The highly ordered distribution of neurons is an essential feature of a functional mammalian retina. Disruptions in the apico-basal polarity complexes at the outer limiting membrane (OLM) of the retina are associated with retinal patterning defects in vertebrates. We have analyzed the binding repertoire of MPP5/Pals1, a key member of the apico-basal Crumbs polarity complex, that has functionally conserved counterparts in zebrafish (nagie oko) and Drosophila (Stardust). We show that MPP5 interacts with its MAGUK family member MPP1/p55 at the OLM. Mechanistically, this interaction involves heterodimerization of both MAGUK mo…

Scaffold proteinanimal structuresGenetics and epigenetic pathways of disease [NCMLS 6]BioinformaticsPDZ domainMolecular Sequence DataMice TransgenicNerve Tissue ProteinsNeuroinformatics [DCN 3]Models BiologicalRetinaMiceTwo-Hybrid System TechniquesCell polarityPerception and Action [DCN 1]GeneticsNeurosensory disorders [UMCN 3.3]Basal bodyAnimalsHumansAmino Acid SequenceRats WistarEye ProteinsMolecular BiologyZebrafishGenetics (clinical)ActinRenal disorder [IGMD 9]GeneticsExtracellular Matrix ProteinsBinding SitesbiologyModels GeneticCell MembraneMembrane ProteinsGeneral MedicineBlood Proteinsbiology.organism_classificationEmbryo MammalianCell biologyProtein Structure TertiaryRatsGenetic defects of metabolism [UMCN 5.1]Eye disordersense organsCellular energy metabolism [UMCN 5.3]Nucleoside-Phosphate KinaseFunctional Neurogenomics [DCN 2]Neural developmentHuman Molecular Genetics
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IRSp53 controls plasma membrane shape and polarized transport at the nascent lumen in epithelial tubules.

2020

It is unclear whether the establishment of apical–basal cell polarity during the generation of epithelial lumens requires molecules acting at the plasma membrane/actin interface. Here, we show that the I-BAR-containing IRSp53 protein controls lumen formation and the positioning of the polarity determinants aPKC and podocalyxin. Molecularly, IRSp53 acts by regulating the localization and activity of the small GTPase RAB35, and by interacting with the actin capping protein EPS8. Using correlative light and electron microscopy, we further show that IRSp53 ensures the shape and continuity of the opposing plasma membrane of two daughter cells, leading to the formation of a single apical lumen. G…

ScienceSialoglycoproteinsQCell MembraneCell PolarityEpithelial CellsNerve Tissue ProteinsApicobasal polaritySettore MED/08 - Anatomia PatologicaActins Cell Membrane Cell Polarity Epithelial Cells Female Morphogenesis Nerve Tissue Proteins Protein Transport Sialoglycoproteins rab GTP-Binding ProteinsActinsArticleProtein Transportrab GTP-Binding ProteinsMorphogenesisHumanslcsh:QFemalelcsh:ScienceNature communications
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IRSp53 shapes the plasma membrane and controls polarized transport at the nascent lumen during epithelial morphogenesis

2019

AbstractEstablishment of apical–basal cell polarity is necessary for generation of luminal and tubular structures during epithelial morphogenesis. Molecules acting at the membrane/ actin interface are expected to be crucial in governing these processes. Here, we show that the I-BAR-containing IRSp53 protein is restricted to the luminal side of epithelial cells of various glandular organs, and is specifically enriched in renal tubules in human, mice, and zebrafish. Using three-dimensional cultures of renal MDCK and intestinal Caco-2 cysts, we show that IRSp53 is recruited early after the first cell division along the forming apical lumen, and is essential for formation of a single lumen and …

Settore MED/04 - Patologia GeneraleCell divisionbiologyChemistryCytoplasmCell polarityMorphogenesisApical membranebiology.organism_classificationZebrafishActinLumen (unit)Cell biology
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Apical transport of osteopontin is independent of N-glycosylation and sialylation.

2002

Studies of how epithelial surface polarity into apical and basolateral domains is generated and maintained have proposed that carbohydrate modifications serve as apical targeting signals for proteins by interacting with lectin sorters. However, the experimental evidence in support of N-glycans, O-glycans and sialic acids mediating apical transport is still very controversial. This could be partly due to the fact that in most studies exogenously expressed proteins were analysed. One has, therefore, examined the role of carbohydrate moieties in apical targeting of the endogenous secretory protein osteopontin in MDCK cells. It was found, however, that sorting of osteopontin does not require N-…

Signal peptideAcetylgalactosamineGlycosylationProtein ConformationSialoglycoproteinsOligosaccharidesBiologyProtein Sorting SignalsKidneyCell Linechemistry.chemical_compoundDogsN-linked glycosylationLectinsCell polarityBenzyl CompoundsAnimalsOsteopontinMolecular BiologyCell PolarityEpithelial CellsCell BiologySialic acidTransport proteincarbohydrates (lipids)Molecular WeightProtein TransportProtein Sorting SignalsSecretory proteinchemistryBiochemistrybiology.proteinSialic AcidsOsteopontinMolecular membrane biology
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