Search results for "BiFC"

showing 3 items of 3 documents

Thioredoxin (Trxo1) interacts with proliferating cell nuclear antigen (PCNA) and its overexpression affects the growth of tobacco cell culture.

2017

Thioredoxins (Trxs), key components of cellular redox regulation, act by controlling the redox status of many target proteins, and have been shown to play an essential role in cell survival and growth. The presence of a Trx system in the nucleus has received little attention in plants, and the nuclear targets of plant Trxs have not been conclusively identified. Thus, very little is known about the function of Trxs in this cellular compartment. Previously, we studied the intracellular localization of PsTrxo1 and confirmed its presence in mitochondria and, interestingly, in the nucleus under standard growth conditions. In investigating the nuclear function of PsTrxo1 we identified proliferati…

0106 biological sciences0301 basic medicineTFs transcription factorsOverexpressionBiologíaBiFC bimolecular fluorescence complementationClinical BiochemistryCell Culture TechniquesTobacco BY-2 cells01 natural sciencesBiochemistryTBY-2 tobacco bright yellow-2DTT 14-dithiothreitolBimolecular fluorescence complementationThioredoxinsGene Expression Regulation PlantTrx thioredoxinlcsh:QH301-705.5GFP green fluorescent proteinlcsh:R5-920biologyProliferating cell nuclear antigen (PCNA)Cell cycleGlutathione3. Good healthCell biologyMitochondriaNTR NADPH thioredoxin reductaseProtein TransportDEM diethyl maleateRT-qPCR Reverse transcription quantitative polymerase chain reactionThioredoxinlcsh:Medicine (General)Oxidation-ReductionAMS 4-acetamido-4-maleimidylstilbene-22-disulfonic acidResearch PaperPCNA proliferating cell nuclear antigenOex overexpressingCell cycleNucleusThioredoxin o103 medical and health sciencesROS reactive oxygen speciesDownregulation and upregulationProliferating Cell Nuclear AntigenTobaccoDAPI 46-diamidine-2-phenylindolmCBM monochlorobimaneCellular compartmentCell NucleusCell growthOrganic ChemistryBotánicaPeasMolecular biologyYFP yellow fluorescent proteinProliferating cell nuclear antigenTBS Tris-buffered salineOD optical density030104 developmental biologylcsh:Biology (General)Cell cultureRNA reactive nitrogen speciesbiology.proteinPrx peroxiredoxinBSA bovine serum albumin010606 plant biology & botanyRedox biology
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The cytoprotective protein MANF promotes neuronal survival independently from its role as a GRP78 cofactor

2021

Mesencephalic astrocyte-derived neurotrophic factor (MANF) is an endoplasmic reticulum (ER)-stress-regulated protein exhibiting cytoprotective properties through a poorly understood mechanism in various in vitro and in vivo models of neuronal and non-neuronal damage. Although initially characterized as a secreted neurotrophic factor for midbrain dopamine neurons, MANF has recently gained more interest for its intracellular role in regulating the ER homeostasis, including serving as a cofactor of the chaperone glucose-regulated protein 78 (GRP78). We aimed for a better understanding of the neuroprotective mechanisms of MANF. Here we show for the first time that MANF promotes the survival of …

0301 basic medicineBiFC bimolecular fluorescence complementationMST microscale thermophoresisPDIA1 protein disulfide isomerase family A member 1ApoptosisNEUROTROPHIC FACTOR MANFEndoplasmic ReticulumBiochemistryprotein-protein interactionMiceBimolecular fluorescence complementationUPR unfolded protein responseENDOPLASMIC-RETICULUM STRESSMesencephalonNeurotrophic factorsInsulin-Secreting CellsProtein Interaction MappingBINDINGCOMPREHENSIVE RESOURCEATF6unfolded protein response (UPR)PDIA6 protein disulfide isomerase family A member 6PPIs protein-protein interactionsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsNPTN neuroplastinbiologyChemistryapoptosisunfolded protein responsedopamine neurons3. Good healthCell biologyGDNF glial cell line–derived neurotrophic factorIRE1-ALPHASBD substrate-binding domainendoplasmic reticulum stressMANF mesencephalic astrocyte-derived neurotrophic factorTm tunicamycinneuroprotectionResearch ArticleProtein BindingSignal TransductionGRP78Protein Disulfide-Isomerase FamilyCell SurvivalTH tyrosine hydroxylasePrimary Cell CultureSCG superior cervical ganglionProtein Disulfide-IsomerasesIRE1 inositol-requiring enzyme 1ER-STRESSER endoplasmic reticulum03 medical and health sciencesohjelmoitunut solukuolemaC-MANF C-terminal domain of MANFCSPs chemical shift perturbationsAnimalsHumansHSP70 Heat-Shock ProteinsNerve Growth FactorsNBD nucleotide-binding domainNMR nuclear magnetic resonanceMolecular Biology030102 biochemistry & molecular biologyBIPATF6Dopaminergic NeuronsGene Expression ProfilingBinding proteinneuronal cell deathDISSOCIATIONCell BiologyNEI nucleotide exchange inhibitorEmbryo MammalianadenosiinitrifosfaattiATPhermosolutmesencephalic astrocyte-derived neurotrophic factorprotein–protein interactionPERK protein kinase RNA-like ER kinaseHEK293 Cells030104 developmental biologyGene Expression RegulationChaperone (protein)Tg thapsigarginbiology.proteinUnfolded protein responseAP-MS affinity purification mass spectrometry1182 Biochemistry cell and molecular biologyGFP-SH SH-tagged GFPendoplasmic reticulum stress (ER stress)DA dopaminemesencephalic astrocyte-derived neurotrophic factor (MANF)proteiinitNeuroplastin
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Inhibitory activities of short linear motifs underlie Hox interactome specificity in vivo

2015

Hox proteins are well-established developmental regulators that coordinate cell fate and morphogenesis throughout embryogenesis. In contrast, our knowledge of their specific molecular modes of action is limited to the interaction with few cofactors. Here, we show that Hox proteins are able to interact with a wide range of transcription factors in the live Drosophila embryo. In this context, specificity relies on a versatile usage of conserved short linear motifs (SLiMs), which, surprisingly, often restrains the interaction potential of Hox proteins. This novel buffering activity of SLiMs was observed in different tissues and found in Hox proteins from cnidarian to mouse species. Although th…

Embryo Nonmammalian[SDV]Life Sciences [q-bio]Amino Acid MotifsinteractomeInteractomeBimolecular fluorescence complementationMiceTARGET GENEDrosophila ProteinsCELL REGULATIONProtein Interaction MapsBiology (General)Hox genetranscription factorGeneticsD. melanogasterGeneral NeuroscienceQRINTERACTION MODULESGeneral MedicineREGIONSHoxTRANSCRIPTION FACTORSDrosophila melanogasterGenomics and Evolutionary BiologyOrgan Specificityembryonic structuresMedicineOligopeptidesProtein BindingResearch Articleanimal structuresQH301-705.5ScienceembryoContext (language use)Computational biology[SDV.BC]Life Sciences [q-bio]/Cellular BiologyCell fate determinationBiologyBinding CompetitiveGeneral Biochemistry Genetics and Molecular BiologyFluorescenceProtein–protein interactionEvolution MolecularStructure-Activity Relationship[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyAnimalsShort linear motif[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyBiFCTranscription factor[SDV.BC] Life Sciences [q-bio]/Cellular BiologydevelopmentHomeodomain ProteinsABDOMINAL-AGeneral Immunology and MicrobiologyBIMOLECULAR FLUORESCENCE COMPLEMENTATIONREPRESSIONDNAPROTEIN INTERACTIONSIntrinsically Disordered ProteinsDROSOPHILA-MELANOGASTERMutationeLife
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