Search results for "microtubule-associated proteins"

showing 10 items of 104 documents

Survivin’s Dual Role: An Export’s View

2007

Survivin is proposed to function as a mitotic regulator and an apoptosis inhibitor during development and pathogenesis. As such, survivin has aroused keen interest in disparate areas of basic and translational research. Survivin acts as a subunit of the chromosomal passenger complex (CPC), composed of the mitotic kinase Aurora-B, Borealin and INCENP, and is essential for proper chromosome segregation and cytokinesis. Our recent findings indicate that the nuclear export receptor Crm1 is critically involved in tethering the CPC to the centromere by interacting with a leucine-rich nuclear export signal (NES), evolutionary conserved in all mammalian survivin proteins. In addition, the survivin/…

Cell NucleusApoptosis InhibitorINCENPSurvivinActive Transport Cell NucleusCell BiologyCell cycleBiologyInhibitor of Apoptosis ProteinsNeoplasm ProteinsCell biologySurvivinAnimalsHumansNuclear export signalMicrotubule-Associated ProteinsneoplasmsMolecular BiologyMitosisCytokinesisNuclear localization sequenceDevelopmental BiologyCell Cycle
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Identification of an Antigen Related to the Sea Urchin RNA-Binding Protein LP54 in Mammalian Central Nervous System

2001

LP54 is an RNA-binding protein involved in localization of maternal messengers in sea urchin egg and embryos. Using a polyclonal antibody directed against Paracentrotus lividus LP54 we detected a 66-kDa cross-reacting antigen in undifferentiated and differentiated SH-SY5Y human neuroblastoma cells. After treatment of undifferentiated cells with detergent, the 66-kDa antigen was found to be enriched in the cytoskeletal fraction. By Western blot the expression of this antigen was also analyzed in regions of the CNS and in tissues of the adult rat and its exclusive presence in the hippocampus and thalamus was revealed. The immunoreactivity with P. lividus antibody against LP54 in hippocampal l…

Central Nervous SystemRNA localizationOctoxynolBlotting WesternDetergentsRNA-binding proteinBinding CompetitiveHippocampusParacentrotus lividusThalamusWestern blotAntigenbiology.animalTumor Cells CulturedmedicineAnimalsHumansRNA MessengerMolecular BiologySea urchinCytoskeletonbiologymedicine.diagnostic_testRNA-Binding ProteinsCell Differentiationbiology.organism_classificationMolecular biologyRatsMicroscopy FluorescencePolyclonal antibodiesSea Urchinsbiology.proteinElectrophoresis Polyacrylamide GelAntibodyMicrotubule-Associated ProteinsMolecular Cell Biology Research Communications
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Kif3a interacts with Dynactin subunit p150 Glued to organize centriole subdistal appendages.

2013

Formation of cilia, microtubule-based structures that function in propulsion and sensation, requires Kif3a, a subunit of Kinesin II essential for intraflagellar transport (IFT). We have found that, Kif3a is also required to organize centrioles. In the absence of Kif3a, the subdistal appendages of centrioles are disorganized and lack p150(Glued) and Ninein. Consequently, microtubule anchoring, centriole cohesion and basal foot formation are abrogated by loss of Kif3a. Kif3a localizes to the mother centriole and interacts with the Dynactin subunit p150(Glued) . Depletion of p150(Glued) phenocopies the effects of loss of Kif3a, indicating that Kif3a recruitment of p150(Glued) is critical for s…

CentrioleKnockoutKinesinsBiologycentriole cohesionKif3aMedical and Health SciencesArticleGeneral Biochemistry Genetics and Molecular BiologyMiceMicrotubuleIntraflagellar transportInformation and Computing SciencesAnimalsHumansKIF3AMicrotubule anchoringMolecular BiologyCentriolesMice KnockoutGeneral Immunology and MicrobiologyGeneral NeuroscienceCiliumTumor Suppressor ProteinsNuclear ProteinsKinesinDynactin ComplexBiological SciencesCell biologyCytoskeletal ProteinscentrosomeCentrosomeHela CellsDynactinGeneric health relevanceMicrotubule-Associated Proteinsp150(Glued)HeLa Cellssubdistal appendageDevelopmental Biology
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Dual effects of increased glycogen synthase kinase-3β activity on adult neurogenesis

2013

Adult neurogenesis, the generation of new neurons during the adulthood, is a process controlled by several kinases and phosphatases among which GSK3β exerts important functions. This protein is particularly abundant in the central nervous system, and its activity deregulation is believed to play a key role in chronic disorders such as Alzheimer's disease. Previously, we reported that in vivo overexpression of GSK3β (Tet/GSK3β mice) causes alterations in adult neurogenesis, leading to a depletion of the neurogenic niches. Here, we have further characterized those alterations, finding a delay in the switching-off of doublecortin marker as well as changes in the survival and death rates of imm…

Chemokine CCL11Doublecortin Domain ProteinsCell SurvivalNeurogenesisTransgeneCentral nervous systemMice TransgenicNerve Tissue ProteinsBiologySubgranular zoneNestinGlycogen Synthase Kinase 3MiceIntermediate Filament ProteinsNeural Stem CellsGenes ReporterGlial Fibrillary Acidic ProteinGeneticsmedicineAnimalsStem Cell NicheMolecular BiologyGSK3BGenetics (clinical)NeuronsGlycogen Synthase Kinase 3 betaNeuropeptidesNeurogenesisNuclear ProteinsGeneral MedicineNestinbeta-GalactosidaseCell biologyDoublecortinDNA-Binding ProteinsMice Inbred C57BLmedicine.anatomical_structureEnzyme InductionDentate GyrusImmunologybiology.proteinMicrotubule-Associated ProteinsNeural developmentBiomarkersHuman Molecular Genetics
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A p16INK4a-insensitive CDK4 mutant targeted by cytolytic T lymphocytes in a human melanoma.

1995

A mutated cyclin-dependent kinase 4 (CDK4) was identified as a tumor-specific antigen recognized by HLA-A2. 1-restricted autologous cytolytic T lymphocytes (CTLs) in a human melanoma. The mutated CDK4 allele was present in autologous cultured melanoma cells and metastasis tissue, but not in the patient's lymphocytes. The mutation, an arginine-to-cysteine exchange at residue 24, was part of the CDK4 peptide recognized by CTLs and prevented binding of the CDK4 inhibitor p16INK4a, but not of p21 or of p27KIP1. The same mutation was found in one additional melanoma among 28 melanomas analyzed. These results suggest that mutation of CDK4 can create a tumor-specific antigen and can disrupt the ce…

Cyclin-Dependent Kinase Inhibitor p21Tumor suppressor geneMutantMolecular Sequence DataCell Cycle ProteinsBiologyProtein Serine-Threonine Kinasesmedicine.disease_causeTransfectionPolymerase Chain ReactionMetastasisCell LineAntigenCyclinsProto-Oncogene ProteinsHLA-A2 AntigenmedicineTumor Cells CulturedAnimalsHumansPoint MutationAmino Acid SequenceCloning MolecularneoplasmsMelanomaCyclin-Dependent Kinase Inhibitor p16Cyclin-Dependent Kinase Inhibitor p15MutationMultidisciplinaryintegumentary systemBase SequenceMelanomaTumor Suppressor ProteinsCyclin-Dependent Kinase 4Cell cyclemedicine.diseaseCyclin-Dependent KinasesCytolysisCancer researchCarrier ProteinsMicrotubule-Associated ProteinsCyclin-Dependent Kinase Inhibitor p27T-Lymphocytes CytotoxicScience (New York, N.Y.)
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Nuclear and Cytoplasmic Survivin: Molecular Mechanism, Prognostic, and Therapeutic Potential.

2007

Abstract Survivin's proposed dual role as an apoptosis inhibitor and a mitotic effector positioned it in the front line of cancer research. Notably, survivin is detected as a cytoplasmic and nuclear protein in cancer patients, which stimulated numerous studies to investigate and to speculate on the functional and prognostic significance of its dynamic localization. Recent evidence shows that the direct interaction of survivin with the nuclear export receptor Crm1 is critically involved in its intracellular localization and cancer-relevant functions. Here, we review our current understanding of the Crm1/survivin interface and discuss its potential prognostic and therapeutic relevance. [Cance…

CytoplasmCancer ResearchPathologymedicine.medical_specialtyApoptosis InhibitorSurvivinActive Transport Cell NucleusMitosisReceptors Cytoplasmic and NuclearKaryopherinsBiologyModels BiologicalInhibitor of Apoptosis ProteinsNeoplasmsSurvivinmedicineHumansNuclear proteinNuclear export signalReceptorMitosisCell NucleusEffectorCancerPrognosismedicine.diseaseNeoplasm ProteinsGene Expression Regulation NeoplasticOncologyCancer researchMicrotubule-Associated ProteinsBiologie
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Dynamic intracellular survivin in oral squamous cell carcinoma: underlying molecular mechanism and potential as an early prognostic marker

2007

Survivin functions as an apoptosis inhibitor and a regulator of cell division in many tumours. The intracellular localization of survivin in tumours has been suggested as a prognostic marker. However, current reports are inconsistent and the underlying molecular mechanisms are not understood. The present study has examined the localization and prognostic value of nuclear and cytoplasmic survivin in the pre-therapeutic biopsies from 71 oral and oropharyngeal squamous carcinoma (OSCC) patients. Statistical analysis indicated that preferential nuclear versus cytoplasmic survivin correlated with favourable versus unfavourable disease outcome. Uni- and multi-variate analysis showed that in contr…

CytoplasmProgrammed cell deathPathologymedicine.medical_specialtySurvivinReceptors Cytoplasmic and NuclearApoptosisKaplan-Meier EstimateCysteine Proteinase InhibitorsKaryopherinsInhibitor of Apoptosis ProteinsPathology and Forensic MedicineCell Line TumorSurvivinBiomarkers TumorCarcinomaHumansMedicineNuclear export signalneoplasmsCell NucleusNuclear Export SignalsPredictive markerbusiness.industryCell cyclePrognosismedicine.diseaseImmunohistochemistryNeoplasm ProteinsSquamous carcinomaOropharyngeal NeoplasmsHead and Neck NeoplasmsApoptosisCarcinoma Squamous CellCancer researchMouth NeoplasmsbusinessMicrotubule-Associated ProteinsThe Journal of Pathology
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Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1.

1999

AbstractThe interaction of cytoplasmic dynein with its cargoes is thought to be indirectly mediated by dynactin, a complex that binds to the dynein intermediate chain. However, the roles of other dynein subunits in cargo binding have been unknown. Here we demonstrate that dynein translocates rhodopsin-bearing vesicles along microtubules. This interaction occurs directly between the C-terminal cytoplasmic tail of rhodopsin and Tctex-1, a dynein light chain. C-terminal rhodopsin mutations responsible for retinitis pigmentosa inhibit this interaction. Our results point to an alternative docking mechanism for cytoplasmic dynein, provide novel insights into the role of motor proteins in the pola…

CytoplasmRhodopsingenetic structuresMicrotubule-associated proteinRecombinant Fusion ProteinsDyneinMolecular Sequence DataReceptors Cell Surfacemacromolecular substancesBiologyT-Complex Genome RegionMicrotubulesGeneral Biochemistry Genetics and Molecular BiologyMotor protein03 medical and health sciencesMice0302 clinical medicineMicrotubuleAnimalsAmino Acid Sequence030304 developmental biologyt-Complex Genome Region0303 health sciencesBinding SitesBiochemistry Genetics and Molecular Biology(all)DyneinsNuclear ProteinsBiological Transport3. Good healthCell biologyCytoplasmRhodopsinMutagenesisDynactinbiology.proteinMicrotubule ProteinsCattlesense organsMicrotubule-Associated Proteins030217 neurology & neurosurgeryPhotoreceptor Cells VertebrateCell
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Cellular Plasticity in the Adult Murine Piriform Cortex: Continuous Maturation of Dormant Precursors Into Excitatory Neurons

2017

Neurogenesis in the healthy adult murine brain is based on proliferation and integration of stem/progenitor cells and is thought to be restricted to 2 neurogenic niches: the subventricular zone and the dentate gyrus. Intriguingly, cells expressing the immature neuronal marker doublecortin (DCX) and the polysialylated-neural cell adhesion molecule reside in layer II of the piriform cortex. Apparently, these cells progressively disappear along the course of ageing, while their fate and function remain unclear. Using DCX-CreERT2/Flox-EGFP transgenic mice, we demonstrate that these immature neurons located in the murine piriform cortex do not vanish in the course of aging, but progressively res…

Doublecortin Domain Proteins0301 basic medicineDoublecortin ProteinCognitive NeuroscienceCell PlasticityGreen Fluorescent ProteinsSubventricular zoneMice TransgenicNerve Tissue ProteinsNeural Cell Adhesion Molecule L1Piriform CortexBiologyMice03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicineCortex (anatomy)Piriform cortexNeuroplasticitymedicineAnimalsNeuronsGlutamate DecarboxylaseStem CellsDentate gyrusNeuropeptidesNeurogenesisGene Expression Regulation DevelopmentalEmbryo MammalianCell biologyDoublecortinMice Inbred C57BL030104 developmental biologymedicine.anatomical_structureBromodeoxyuridinenervous systemSialic Acidsbiology.proteinTBR1Calcium-Calmodulin-Dependent Protein Kinase Type 2Microtubule-Associated Proteins030217 neurology & neurosurgeryCerebral Cortex
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Extensive migration of young neurons into the infant human frontal lobe

2016

Building the human brain As the brain develops, neurons migrate from zones of proliferation to their final locations, where they begin to build circuits. Paredes et al. have discovered that shortly after birth, a group of neurons that proliferates near the ventricles migrates in chains alongside circulatory vessels into the frontal lobes (see the Perspective by McKenzie and Fishell). Young neurons that migrate postnatally into the anterior cingulate cortex then develop features of inhibitory interneurons. The number of migratory cells decreases over the first 7 months of life, and by 2 years of age, migratory cells are not evident. Any damage during migration, such as hypoxia, may affect th…

Doublecortin Domain Proteins0301 basic medicineNeurogenesisNeuropeptideBiologyInhibitory postsynaptic potentialGyrus Cinguli03 medical and health sciencesLateral ventricles0302 clinical medicineCell MovementInterneuronsLateral VentriclesCorrespondenceNeuroplasticitymedicineHumansGyrus cinguliAnterior cingulate cortexNeuronsNeuronal PlasticityMultidisciplinaryNeuropeptidesNeurogenesisInfantAnatomyFrontal Lobe030104 developmental biologymedicine.anatomical_structureFrontal lobeMicrotubule-Associated Proteins030217 neurology & neurosurgeryScience
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