Search results for "calcium-binding"

showing 10 items of 85 documents

The b1 isoform of protocadherin-gamma (Pcdhgamma) interacts with the microtubule-destabilizing protein SCG10.

2004

Due to their structural characteristics and their diversity, the 22 members of the protocadherin-gamma (Pcdhgamma) family have been suggested to contribute to the establishment of specific connections in the nervous system. Here, we focus on a single isoform, Pcdhgamma-b1. Its expression is found in different brain regions and in developing spinal cord it is restricted to scattered cells, whereas all cells are labeled using an antibody that recognizes all Pcdhgamma isoforms. As a first step to understanding the signaling mechanisms downstream of Pcdhgamma, we identify the microtubule-destabilizing protein SCG10 as a cytoplasmic interactor for Pcdhgamma-b1 and other isoforms of the Pcdhgamma…

Gene isoformNervous systemSubfamilyRecombinant Fusion ProteinsBiophysicsTwo-hybridProtocadherinCadherin Related ProteinsBiologyBiochemistryMicrotubulesMiceProtocadherinStructural BiologyMicrotubuleTwo-Hybrid System TechniquesChlorocebus aethiopsGeneticsmedicineAnimalsProtein IsoformsInteractorNerve Growth FactorsGrowth coneMolecular BiologyNeuronsProtocadherin-gammaCalcium-Binding ProteinsIntracellular Signaling Peptides and ProteinsBrainCell BiologySCGIOCadherinsMolecular biologyCell biologySCG10medicine.anatomical_structureCytoplasmCOS CellsStathminGrowth coneSignal TransductionFEBS letters
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Centrins, gatekeepers for the light-dependent translocation of transducin through the photoreceptor cell connecting cilium

2006

Centrins are members of a highly conserved subgroup of the EF-hand superfamily of Ca(2+)-binding proteins commonly associated with centrosome-related structures. In the retina, centrins are also prominent components of the photoreceptor cell ciliary apparatus. Centrin isoforms are differentially localized at the basal body and in the lumen of the connecting cilium. All molecular exchanges between the inner and outer segments occur through this narrow connecting cilium. Ca(2+)-activated centrin isoforms bind to the visual heterotrimeric G-protein transducin via an interaction with the betagamma-subunit. Ca(2+)-dependent assemblies of centrin/G-protein complexes may regulate the transducin mo…

Gene isoformPhotoreceptorsgenetic structuresPhotoreceptor cellHeterotrimeric G proteinConnecting ciliummedicineCentrinBasal bodyAnimalsPhotoreceptor CellsCiliaTransducinPhosphorylationVision OcularCentrosomeRetinaChemistryLight-dependent translocationCiliumCalcium-Binding ProteinsSensory SystemsCell biologyProtein TransportOphthalmologymedicine.anatomical_structureCentrinVertebratesTransducinsense organsPhotic StimulationVision Research
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Centrins in retinal photoreceptor cells: regulators in the connecting cilium.

2008

Changes in the intracellular Ca2+ concentration regulate the visual signal transduction cascade directly or more often indirectly through Ca2+-binding proteins. Here we focus on centrins, which are members of a highly conserved subgroup of the EF-hand superfamily of Ca2+-binding proteins in photoreceptor cells of the vertebrate retina. Centrins are commonly associated with centrosome-related structures. In mammalian retinal photoreceptor cells, four centrin isoforms are expressed as prominent components in the connecting cilium linking the light-sensitive outer segment compartment with the metabolically active inner segment compartment. Our data indicate that Ca2+-activated centrin isoforms…

Gene isoformgenetic structuresChromosomal Proteins Non-HistoneBiologyContractile ProteinsHeterotrimeric G proteinmedicineCompartment (development)AnimalsHumansCiliaEye ProteinsVision OcularRetinaCalcium-Binding ProteinsSensory SystemsCell biologyOphthalmologymedicine.anatomical_structureCentrinCalciumsense organsTransducinSignal transductionIntracellularPhotoreceptor Cells VertebrateProgress in retinal and eye research
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MAD2 depletion triggers premature cellular senescence in human primary fibroblasts by activating a P53 pathway preventing aneuploid cells propagation.

2012

The spindle assembly checkpoint (SAC) is a cellular surveillance mechanism that ensures faithful chromosome segregation during mitosis and its failure can result in aneuploidy. Previously, it was suggested that reduction of the MAD2 gene, encoding a major component of the SAC, induced aneuploidy in human tumor cells. However, tumor cell lines contain multiple mutations that might affect or exacerbate the cellular response to Mad2 depletion. Thus, the scenario resulting by Mad2 depletion in primary human cells could be different and more complex that the one depicted so far. We used primary human fibroblasts (IMR90) and epithelial breast cells (MCF10A) to gain further insight on the effects …

Genome instabilityCyclin-Dependent Kinase Inhibitor p21Cell cycle checkpointMad2PhysiologyClinical BiochemistryMAD2 depletion Aneuploidy Premature cellular senescence TP53Cell Cycle ProteinsBiologyCyclin-dependent kinaseChromosome instabilityChromosomal InstabilityTumor Suppressor Protein p14ARFHumansGene SilencingRNA Small InterferingMitosisCells CulturedCellular SenescenceCell ProliferationCalcium-Binding ProteinsCell BiologyCell Cycle CheckpointsFibroblastsAneuploidybeta-GalactosidaseCell biologyRepressor ProteinsSpindle checkpointSettore BIO/18 - GeneticaGene Expression RegulationMad2 Proteinsbiology.proteinM Phase Cell Cycle CheckpointsTumor Suppressor Protein p53Cell agingSignal Transduction
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Role for calnexin and N-linked glycosylation in the assembly and secretion of hepatitis B virus middle envelope protein particles.

1998

ABSTRACT Unlike those of the S and the L envelope proteins, the functional role of the related M protein in the life cycle of the hepatitis B virus (HBV) is less understood. We now demonstrate that a single N glycan, specific for M, is required for efficient secretion of M empty envelope particles. Moreover, this glycan mediates specific association of M with the chaperone calnexin. Conversely, the N glycan, common to all three envelope proteins, is involved neither in calnexin binding nor in subviral particle release. As proper folding and trafficking of M need the assistance of the chaperone, the glycan-dependent association of M with calnexin may thus play a crucial role in the assembly …

GlycanHepatitis B virusGlycosylationGlycosylationCalnexinImmunologyBiologymedicine.disease_causeMicrobiologychemistry.chemical_compoundCytosolN-linked glycosylationViral Envelope ProteinsVirologyCalnexinmedicineAnimalsSecretionPeptide sequenceHepatitis B virusBase SequenceCalcium-Binding ProteinsVirus-Cell Interactionscarbohydrates (lipids)BiochemistrychemistryOligodeoxyribonucleotidesInsect ScienceChaperone (protein)COS Cellsbiology.proteinMutagenesis Site-DirectedJournal of virology
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The hematopoietic niche: a Drosophila model, at last.

2007

The niche provides a specialised microenvironment necessary for maintenance of stem cells in a non differentiated state. While the hematopoietic stem cell (HSC) niche in vertebrates was the first to be recognized, Drosophila niches supporting germline stem cells were characterised first. Recent evidence for the existence of a niche maintaining hematopoietic precursors in Drosophila opens the way to study in vivo the niche/hematopoietic precursors interactions. The availability of a large collection of cell markers, mutants and sophisticated genetic tools makes Drosophila an attractive model for investigating the cellular and molecular mechanisms that are involved in these interactions.

HemocytesCalcium-Binding ProteinsMembrane ProteinsHematopoietic Stem CellsLarvaModels Animal[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyAnimalsDrosophila ProteinsIntercellular Signaling Peptides and Proteins[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyDrosophilaSerrate-Jagged Proteins[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyBiomarkersJagged-1 ProteinTranscription FactorsCell cycle (Georgetown, Tex.)
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Chaperones Involved in Hepatitis B Virus Morphogenesis

1999

Little is known about host cell factors necessary for hepatitis B virus (HBV) assembly which involves envelopment of cytosolic nucleocapsids by the S, M and L transmembrane viral envelope proteins and subsequent budding into intraluminal cisternae. Central to virogenesis is the L protein that mediates hepatocyte receptor binding and envelopment of capsids. To serve these topologically conflicting roles, L protein exhibits an unusual dual membrane topology, disposing its N-terminal preS domain inside and outside of the virion lipid envelope. The mixed topology is achieved by posttranslational preS translocation of about half of the L protein molecules across a post-endoplasmic reticulum memb…

Hepatitis B virusProtein FoldingCalnexinHSC70 Heat-Shock ProteinsClinical BiochemistryBiochemistryViral Matrix ProteinsCytosolViral Envelope ProteinsViral envelopeCalnexinMorphogenesisAnimalsHumansHSP70 Heat-Shock ProteinsProtein PrecursorsMolecular BiologyHepatitis B Surface AntigensViral matrix proteinbiologyChemistryCalcium-Binding ProteinsHSC70 Heat-Shock ProteinsBiological TransportVirologyTransmembrane proteinCell biologyProtein BiosynthesisMembrane topologyChaperone (protein)COS Cellsbiology.proteinProtein foldingCarrier ProteinsMolecular ChaperonesBiological Chemistry
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The Expanding Spectrum of Mutations in Hereditary Angioedema.

2021

The evolution in the knowledge of rare genetic diseases such as hereditary angioedema (HAE) has increased at a parallel pace with the development of new molecular tools. The deficiency of C1 inhibitor (C1-INH) has been recognized as the main cause of HAE (HAE-C1-INH) since the 1960s, but the discovery of the wide spectrum of mutations affecting the C1-INH gene (SERPING1) was possible only from the late 1980s, when Sanger sequencing became available and more accessible worldwide. Nevertheless, the involvement of other genes in HAE was discovered only in 2006 with the description of mutations in the F12 gene in patients with HAE and normal C1-INH. In the last 3 years, advanced next-generation…

Kininogen 1Muscle ProteinsGenomicsSeverity of Illness IndexDNA sequencingC1-inhibitorPathogenesis03 medical and health sciencessymbols.namesake0302 clinical medicineImmunology and AllergyMedicineHumans030212 general & internal medicineGeneSanger sequencingGeneticsbiologybusiness.industryCalcium-Binding ProteinsAngioedemas HereditaryMembrane Proteinsmedicine.disease030228 respiratory systemHereditary angioedemaMutationbiology.proteinsymbolsbusinessComplement C1 Inhibitor ProteinThe journal of allergy and clinical immunology. In practice
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Calcium-Dependent Assembly of Centrin-G-Protein Complex in Photoreceptor Cells

2002

Photoexcitation of rhodopsin activates a heterotrimeric G-protein cascade leading to cyclic GMP hydrolysis in vertebrate photoreceptors. Light-induced exchanges of the visual G-protein transducin between the outer and inner segment of rod photoreceptors occur through the narrow connecting cilium. Here we demonstrate that transducin colocalizes with the Ca(2+)-binding protein centrin 1 in a specific domain of this cilium. Coimmunoprecipitation, centrifugation, centrin overlay, size exclusion chromatography, and kinetic light-scattering experiments indicate that Ca(2+)-activated centrin 1 binds with high affinity and specificity to transducin. The assembly of centrin-G-protein complex is medi…

Lightgenetic structuresChromosomal Proteins Non-HistoneMacromolecular SubstancesImmunoprecipitationG proteinCentrifugationPlasma protein bindingBiologyRetinaSubstrate SpecificityRats Sprague-DawleyMiceHeterotrimeric G proteinCalcium-binding proteinAnimalsScattering RadiationTransducinMicroscopy ImmunoelectronCell Growth and DevelopmentMolecular BiologyCalcium-Binding ProteinsCell BiologyHeterotrimeric GTP-Binding ProteinsPrecipitin TestsRatsCell biologyMice Inbred C57BLMolecular WeightRhodopsinCentrinChromatography Gelbiology.proteinCalciumCattlesense organsTransducinPhotoreceptor Cells VertebrateProtein BindingSignal TransductionMolecular and Cellular Biology
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Histocompatibility reaction in tissue and cells of the marine sponge Suberites domuncula in vitro and in vivo: central role of the allograft inflamma…

2001

Sponges (Porifera) are the phylogenetically oldest still extant metazoan phylum. Recently elements of their immune system have been cloned and analyzed, primarily from the demosponges Suberites domuncula and Geodia cydonium. By differential display, two genes were identified in S. domuncula, whose translation products are involved in graft rejection/fusion: the allograft inflammatory factor (AIF-1) and the Tcf-like transcription factor (TCF). Since the AIF-1 and TCF genes are upregulated in vivo after tissue transplantation, especially in allografts, we investigated whether this reaction can be monitored in vitro. Therefore, the autogeneic and the allogeneic mixed sponge cell reaction (MSCR…

Lymphoid Enhancer-Binding Factor 1ImmunologyMolecular Sequence DataTacrolimusdemosponges; Suberites domuncula; Geodia cydonium; AIF-1(allograft inflamatory factor 1); TCFMicrobiologyImmune systemGeneticsAnimalsAmino Acid SequenceCloning MoleculareducationTranscription factorPhylogenyeducation.field_of_studyDifferential displaybiologyCalcium-Binding Proteinsbiology.organism_classificationIn vitroRecombinant ProteinsCell biologyHistocompatibilityPoriferaSuberites domunculaDNA-Binding ProteinsSpongeGene Expression RegulationHMG-Box DomainsHistocompatibilityAllograft inflammatory factor 1Transcription Factors
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