Search results for "isoform"

showing 10 items of 350 documents

A GFP-tagged Muscleblind C protein isoform reporter construct

2010

Drosophila muscleblind (mbl), the ortholog of human Muscleblind-like 1 (MBNL1) gene involved in Myotonic Dystrophy (DM), gives raise to protein isoforms MblA to G. The specific functions and subcellular distribution of isoforms are still largely unknown. To overcome the lack of isoform-specific antibodies we generated transgenic flies that express a GFP:MblC fusion protein under the control of the Gal4/UAS system. The reporter fusion protein was able to functionally complement mbl loss of function mutations, demonstrating activity, and accumulated predominantly in adult muscle nuclei. The fluorescent nature of the reporter makes it appropriate for live imaging detection of MblC protein isof…

Cell NucleusProtein isoformGene isoformMusclesRecombinant Fusion ProteinsTransgeneGreen Fluorescent ProteinsNuclear ProteinsBiologyMolecular biologyFusion proteinGreen fluorescent proteinAnimals Genetically Modifiedchemistry.chemical_compoundchemistryGenes ReporterLive cell imagingInsect ScienceAnimalsDrosophila ProteinsMBNL1DrosophilaGenetic EngineeringGeneFly
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ALS-linked FUS mutations confer loss and gain of function in the nucleus by promoting excessive formation of dysfunctional paraspeckles

2019

Mutations in the FUS gene cause amyotrophic lateral sclerosis (ALS-FUS). Mutant FUS is known to confer cytoplasmic gain of function but its effects in the nucleus are less understood. FUS is an essential component of paraspeckles, subnuclear bodies assembled on a lncRNA NEAT1. Paraspeckles may play a protective role specifically in degenerating spinal motor neurons. However it is still unknown how endogenous levels of mutant FUS would affect NEAT1/paraspeckles. Using novel cell lines with the FUS gene modified by CRISPR/Cas9 and human patient fibroblasts, we found that endogenous levels of mutant FUS cause accumulation of NEAT1 isoforms and paraspeckles. However, despite only mild cytoplasm…

Cell NucleusResearchAmyotrophic Lateral SclerosisIntranuclear Inclusion BodiesNEAT1lcsh:RC346-429Cell LineLoss of Function MutationCell Line TumorFused in sarcoma (FUS)ParaspeckleHumansProtein IsoformsRNA-Binding Protein FUSRNA Long NoncodingAmyotrophic lateral sclerosis (ALS)CRISPR-Cas Systemslcsh:Neurology. Diseases of the nervous systemActa Neuropathologica Communications
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Impact of Ultrabithorax alternative splicing on Drosophila embryonic nervous system development.

2015

Hox genes control divergent segment identities along the anteroposterior body axis of bilateral animals by regulating a large number of processes in a cell context-specific manner. How Hox proteins achieve this functional diversity is a long-standing question in developmental biology. In this study we investigate the role of alternative splicing in functional specificity of the Drosophila Hox gene Ultrabithorax (Ubx). We focus specifically on the embryonic central nervous system (CNS) and provide a description of temporal expression patterns of three major Ubx isoforms during development of this tissue. These analyses imply distinct functions for individual isoforms in different stages of n…

Central Nervous SystemEmbryologyanimal structuresNeurogenesisGenes InsectBiologyCell fate determinationNeuroblastAnimalsDrosophila ProteinsProtein IsoformsHox geneUltrabithoraxGeneticsHomeodomain ProteinsAlternative splicingGenes HomeoboxGene Expression Regulation DevelopmentalCell biologyAlternative Splicingembryonic structuresRNA splicingDrosophilaNeural developmentDrosophila ProteinDevelopmental BiologyTranscription FactorsMechanisms of development
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RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin

2005

The ORF15 isoform of RPGR (RPGR(ORF15)) and RPGR interacting protein 1 (RPGRIP1) are mutated in a variety of retinal dystrophies but their functions are poorly understood. Here, we show that in cultured mammalian cells both RPGR(ORF15) and RPGRIP1 localize to centrioles. These localizations are resistant to the microtubule destabilizing drug nocodazole and persist throughout the cell cycle. RPGR and RPGRIP1 also co-localize at basal bodies in cells with primary cilia. The C-terminal (C2) domain of RPGR(ORF15) (ORF15(C2)) is highly conserved across 13 mammalian species, suggesting that it is a functionally important domain. Using matrix-assisted laser desorption ionization time-of-flight mas…

CentrioleFluorescent Antibody TechniqueMicechemistry.chemical_compoundChlorocebus aethiopsGuanine Nucleotide Exchange FactorsProtein IsoformsBasal bodyConserved SequenceGenetics (clinical)CentriolesGlutathione Transferaseintegumentary systemNuclear ProteinsExonsGeneral MedicineRetinitis pigmentosa GTPase regulatorImmunohistochemistryNocodazoleCOS CellsNucleophosminCell NucleolusRecombinant Fusion ProteinsMolecular Sequence DataBiologyOpen Reading FramesMicrotubuleTwo-Hybrid System TechniquesGeneticsAnimalsHumansAmino Acid SequenceEye ProteinsMolecular BiologyNucleophosminSequence Homology Amino AcidProteinsPrecipitin TestsMolecular biologyeye diseasesProtein Structure TertiaryMice Inbred C57BLCytoskeletal ProteinschemistryCentrosomeCytoplasmSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationMutationCattleHeLa CellsHuman Molecular Genetics
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Two Latent and Two Hyperstable Polymeric Forms of Human Neuroserpin

2010

AbstractHuman neuroserpin (hNS) is a serine protease inhibitor that belongs to the serpin superfamily and is expressed in nervous tissues. The serpin fold is generally characterized by a long exposed loop, termed the reactive center loop, that acts as bait for the target protease. Intramolecular insertion of the reactive center loop into the main serpin β-sheet leads to the serpin latent form. As with other known serpins, hNS pathological mutants have been shown to accumulate as polymers composed of quasi-native protein molecules. Although hNS polymerization has been intensely studied, a general agreement about serpin polymer organization is still lacking. Here we report a biophysical chara…

Circular dichroismanimal structuresLightmedicine.medical_treatmenthuman neuroserpinBiophysicsContext (language use)SerpinProtein Structure SecondaryserpinopathiePolymerizationNeuroserpinSpectroscopy Fourier Transform InfraredmedicineHumansProtein IsoformsScattering Radiationpathological serpin aggregationReactive centerSerpinsProtein UnfoldingSerine proteaseProteasebiologyProtein StabilityChemistryCircular DichroismProteinNeuropeptidesTemperatureserpinlatent neuroserpinSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)PolymerizationBiochemistryFENIBembryonic structuresbiology.proteinBiophysicsBiophysical Journal
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Cytotoxic T lymphocytes define multiple peptide isoforms derived from the melanoma-associated antigen MART-1/Melan-A

1999

Peptides derived from the melanoma-associated MART-1/Melan-A antigen are currently implemented in immunotherapy for inducing or augmenting T-cell responses directed against peptides expressed by autologous tumor cells in HLA-A2+ patients with melanoma. Here, we describe the specificity of the T-cell clone SK29-FFM1.1, which secretes GM-CSF in response to a panel of synthetic MART-1/Melan-A-derived peptides, including the naturally presented ILTVILGVL32–40, but exhibits cytotoxicity and IFN-γ secretion exclusively to the MART-1/Melan-A derived peptide AAGIGILTV27–35. In addition, cytotoxic T-lymphocyte (CTL) clone SK29-FFM1.1 recognizes 3 different naturally processed and presented peptides …

Cytotoxicity ImmunologicCancer ResearchCellular immunityReceptors Antigen T-Cell alpha-betaT-Lymphocytesmedicine.medical_treatmentBiologyTransfectionEpitopeInterferon-gammaMART-1 AntigenImmune systemAntigenAntigens NeoplasmHLA-A2 AntigenTumor Cells CulturedmedicineHumansProtein IsoformsCytotoxic T cellAmino Acid SequenceMelanomaneoplasmsintegumentary systemReverse Transcriptase Polymerase Chain ReactionImmunotherapyMolecular biologyRecombinant ProteinsClone CellsNeoplasm ProteinsCTL*OncologyImmunologyClone (B-cell biology)T-Lymphocytes CytotoxicInternational Journal of Cancer
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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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Molecular cloning and expression of Tenebrio molitor ultraspiracle during metamorphosis and in vivo induction of its phosphorylation by 20-hydroxyecd…

2000

Using a RT-PCR approach, the Tenebrio molitor homologue of Drosophila Ultraspiracle (TmUSP) was characterized. Its DNA binding domain shows a degree of identity with those of the other insect USPs. However, the ligand binding domain is closer to those of retinoid X receptors. Using an antibody raised against DmUSP, Western blot analysis of proteins from epidermis and other tissues revealed five immunoreactive bands, corresponding to different phosphorylated forms of a unique polypeptide, as shown by lambda-phosphatase treatment. The nuclear form of TmUSP seems unphosphorylated. An in vivo 20-hydroxyecdysone treatment increases considerably and rapidly the phosphorylated forms of TmUSP. This…

DNA ComplementaryMolecular Sequence Data20-HydroxyecdysoneGene ExpressionMolecular cloningBiologychemistry.chemical_compoundWestern blotGene expressionGeneticsmedicineAnimalsDrosophila ProteinsHumansProtein IsoformsAmino Acid SequenceRNA MessengerCloning MolecularPhosphorylationReceptorTenebrioMolecular BiologyEpidermis (botany)medicine.diagnostic_testMetamorphosis BiologicalDNA-binding domainSequence Analysis DNAMolecular biologyCell biologyDNA-Binding ProteinsEcdysteronechemistryInsect SciencePhosphorylationEpidermisTranscription FactorsInsect molecular biology
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Src proteins/src genes: from sponges to mammals

2004

The genome of marine sponge Suberites domuncula, a member of the most ancient and most simple metazoan phylum Porifera, encodes at least five genes for Src-type proteins, more than, i.e., Caenorhabditis elegans or Drosophila melanogaster (two in each). Three proteins, SRC1SD, SRC2SD and SRC3SD, were fully characterized. The overall homology (identity+similarity) among the three S. domuncula Srcs (68-71%) is much lower than the sequence conservation between orthologous Src proteins from freshwater sponges (82-85%). It is therefore very likely that several src genes/proteins were already present in the genome of Urmetazoa, the hypothetical metazoan ancestor. We have identified in the S. domun…

DNA Complementaryanimal structuresMolecular Sequence DataProto-Oncogene Proteins pp60(c-src)SH2 domainHomology (biology)SH3 domainEvolution Molecularsrc Homology DomainsExonGeneticsAnimalsProtein IsoformsAmino Acid SequenceCloning MolecularGenePhylogenyMammalsGeneticsSequence Homology Amino AcidbiologyIntronDNASequence Analysis DNAGeneral Medicinebiology.organism_classificationIntronsPoriferaSuberites domunculaSequence AlignmentProto-oncogene tyrosine-protein kinase SrcGene
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Low Levels of Acetylcholine Receptor Delta-Subunit Message and Protein in Human Thymus Suggests the Occurrence of ‘Triplet Receptors’ in Thymic Myoid…

2000

Myasthenia gravis (MG) is an autoimmune disease caused by autoantibodies against the acetylcholine receptor (AChR) at the neuromuscular junction [1]. The muscular AChR has been extensively characterized [2], but whether the muscular AChR plays a role during the initiation of MG is unknown [3]. The muscular AChR is a pentameric ion channel composed of 4 different subunits [2, 4]. The fetal AChR expressed during intrauterine life and after denervation of adult muscle exhibits an α2βδγ composition, while the adult AChR expressed after birth in innervated muscle exhibits an α2βδγ composition [4]. The α-subunit contains the main epitopes recognized by MG autoantibodies [2]. The human muscle AChR…

DenervationGene isoformmedicine.medical_specialtyanimal structuresThymomaBiologymusculoskeletal systemmedicine.diseaseMolecular biologyEpitopeMyasthenia gravisNeuromuscular junctionEndocrinologymedicine.anatomical_structureInternal medicinemedicineReceptortissuesAcetylcholine receptor
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