Search results for "Multiprotein complex"

showing 10 items of 42 documents

Small molecule inhibitors of Apaf-1-related caspase- 3/-9 activation that control mitochondrial-dependent apoptosis

2006

10 pages, 5 figures.-- PMID: 16341125 [PubMed].-- Available online Dec 9, 2005.

Multiprotein complexCytochromeProtein-protein interactionsApoptosisCaspase 3MitochondrionLigandsCell LineChemical librarychemistry.chemical_compoundPeptide LibraryApoptosomesPeptoidHumansCombinatorial libraries inhibitorApoptosomeProtein PrecursorsMolecular BiologybiologyCaspase 3Intrinsic apoptosisCytochromes cCell BiologyCaspase InhibitorsCaspase 9Recombinant ProteinsMitochondriaCell biologyEnzyme ActivationCaspasa-9Apoptotic Protease-Activating Factor 1chemistryBiochemistryN-substituted GlycinesApoptosisCaspasa-3biology.proteinApoptosomeApaf-1Molecular recognitionSmall moleculeProtein BindingCell Death & Differentiation
researchProduct

The crystal structure of a 250-kDa heterotetrameric particle explains inhibition of sheddase meprin β by endogenous fetuin-B

2021

Meprin β (Mβ) is a multidomain type-I membrane metallopeptidase that sheds membrane-anchored substrates, releasing their soluble forms. Fetuin-B (FB) is its only known endogenous protein inhibitor. Herein, we analyzed the interaction between the ectodomain of Mβ (MβΔC) and FB, which stabilizes the enzyme and inhibits it with subnanomolar affinity. The MβΔC:FB crystal structure reveals a ∼250-kDa, ∼160-Å polyglycosylated heterotetrameric particle with a remarkable glycan structure. Two FB moieties insert like wedges through a “CPDCP trunk” and two hairpins into the respective peptidase catalytic domains, blocking the catalytic zinc ions through an “aspartate switch” mechanism. Uniquely, the …

Multiprotein complexMetallopeptidaseCleavage (embryo)Cell LineMiceProtein structureAnimalsHumansEctoprotein sheddingProtease InhibitorsInhibitionBinding SitesMultidisciplinarybiologyChemistryMetallopeptidaseMetalloendopeptidasesActive siteBiological SciencesSheddaseFetuin-BLepidopteraMolecular Docking SimulationTransmembrane domainEctodomainbiology.proteinBiophysicsProtein structureMultiprotein complexAlzheimer’s diseaseProtein Binding
researchProduct

Deregulation of the EGFR/PI3K/PTEN/Akt/mTORC1 pathway in breast cancer: possibilities for therapeutic intervention

2014

// Nicole M. Davis 1 , Melissa Sokolosky 1 , Kristin Stadelman 1 , Stephen L. Abrams 1 , Massimo Libra 2 , Saverio Candido 2 , Ferdinando Nicoletti 2 , Jerry Polesel 3 , Roberta Maestro 4 , Antonino D’Assoro 5 , Lyudmyla Drobot 6 , Dariusz Rakus 7 , Agnieszka Gizak 7 , Piotr Laidler 8 , Joanna Dulinska-Litewka 8 , Joerg Basecke 9 , Sanja Mijatovic 10 , Danijela Maksimovic-Ivanic 10 , Giuseppe Montalto 11,12 , Melchiorre Cervello 12 , Timothy L. Fitzgerald 13 , Zoya N. Demidenko 14 , Alberto M. Martelli 15 , Lucio Cocco 15 , Linda S. Steelman 1 and James A. McCubrey 1 1 Department of Microbiology and Immunology, Brody School of Medicine at East Carolina University Greenville, NC 27858 USA 2 …

Oncologymedicine.medical_specialtytherapy resistanceClass I Phosphatidylinositol 3-Kinasesmedicine.medical_treatmentBreast NeoplasmsReviewBiologyMechanistic Target of Rapamycin Complex 1PI3KMetastasisTargeted therapyPhosphatidylinositol 3-KinasesBreast cancerTARGETED THERAPYInternal medicinemedicinePTENHumansTargeted Therapy Therapy Resistance Mutations PI3K mTOR rapamycinskin and connective tissue diseasesProtein kinase BneoplasmsPI3K/AKT/mTOR pathwayRoswell Park Cancer InstituterapamycinTOR Serine-Threonine KinasesMTORPTEN PhosphohydrolaseCancerTargeted TherapyTherapy Resistancemedicine.diseaseTargeted Therapy; Therapy Resistance; Mutations; PI3K; mTOR; rapamycin3. Good healthErbB ReceptorsGene Expression Regulation NeoplasticOncologyMultiprotein ComplexesCancer researchbiology.proteinFemaleReceptor Epidermal Growth FactormutationRAPAMYCINProto-Oncogene Proteins c-aktMutationsSignal Transduction
researchProduct

Htid-1, the human homolog of the Drosophila melanogaster l(2)tid tumor suppressor, defines a novel physiological role of APC.

2007

Htid-1, the human counterpart of the Drosophila tumor suppressor gene lethal(2)tumorous imaginal discs (l(2)tid) encodes three splice forms translated into three cytosolic - Tid50, Tid48 and Tid46 - and three mitochondrial - Tid43, Tid40 and Tid38 - proteins. Here we provide evidence for the association of the endogenous Tid50/Tid48 proteins with the adenomatous polyposis coli (APC) tumor suppressor in normal colon epithelium, colorectal cancer cells and mouse NIH3T3 fibroblasts. Using the Glutathione S-transferase binding assay we show that the N-terminal region including the Armadillo domain (ARM) of APC is sufficient to bind the Tid molecules. Using immunoprecipitation and confocal micro…

Patched ReceptorsBeta-cateninTumor suppressor geneAdenomatous polyposis coliAdenomatous Polyposis Coli ProteinReceptors Cell SurfacePlasma protein bindingLigandsMitochondrial ProteinsMiceCytosolCell Line TumorAnimalsDrosophila ProteinsGuanine Nucleotide Exchange FactorsHumansIntestinal MucosaActinHeat-Shock Proteinsbeta CateninPatched ReceptorsbiologySequence Homology Amino AcidGene Expression ProfilingTumor Suppressor ProteinsWnt signaling pathwayGene Expression Regulation DevelopmentalCell BiologyHSP40 Heat-Shock ProteinsActin cytoskeletonMolecular biologyCell biologyMitochondriaDrosophila melanogasterras GTPase-Activating ProteinsMultiprotein Complexesbiology.proteinNIH 3T3 CellsRho Guanine Nucleotide Exchange FactorsProtein BindingCellular signalling
researchProduct

Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast.

2014

Elongator is a conserved protein complex comprising six different polypeptides that has been ascribed a wide range of functions, but which is now known to be required for modification of uridine residues in the wobble position of a subset of tRNAs in yeast, plants, worms and mammals. In previous work, we showed that Elongator's largest subunit (Elp1; also known as Iki3) was phosphorylated and implicated the yeast casein kinase I Hrr25 in Elongator function. Here we report identification of nine in vivo phosphorylation sites within Elp1 and show that four of these, clustered close to the Elp1 C-terminus and adjacent to a region that binds tRNA, are important for Elongator's tRNA modification…

ProteomicsSaccharomyces cerevisiae Proteinslcsh:QH426-470Saccharomyces cerevisiaeBiochemistryMolecular GeneticsRNA TransferGene Expression Regulation FungalMolecular Cell BiologyGeneticsFungal GeneticsPhosphorylationPost-Translational ModificationUridineMolecular BiologyAdaptor Proteins Signal TransducingHistone AcetyltransferasesAlanineSpectrometric Identification of ProteinsBiology and life sciencesCasein Kinase INucleotidesMicrobial GeneticsProteinsCell BiologyPeptide Elongation Factorslcsh:GeneticsPhenotypeMultiprotein ComplexesRNAMolecular ComplexesTransfer RNAAnticodonsResearch ArticlePLoS genetics
researchProduct

Promoter architecture and transcriptional regulation of Abf1-dependent ribosomal protein genes inSaccharomyces cerevisiae

2016

In Saccharomyces cerevisiae, ribosomal protein gene (RPG) promoters display binding sites for either Rap1 or Abf1 transcription factors. Unlike Rap1-associated promoters, the small cohort of Abf1-dependent RPGs (Abf1-RPGs) has not been extensively investigated. We show that RPL3, RPL4B, RPP1A, RPS22B and RPS28A/B share a common promoter architecture, with an Abf1 site upstream of a conserved element matching the sequence recognized by Fhl1, a transcription factor which together with Ifh1 orchestrates Rap1-associated RPG regulation. Abf1 and Fhl1 promoter association was confirmed by ChIP and/or gel retardation assays. Mutational analysis revealed a more severe requirement of Abf1 than Fhl1 …

Ribosomal Proteins0301 basic medicineSaccharomyces cerevisiae ProteinsTranscription GeneticTelomere-Binding ProteinsRibosome biogenesisSaccharomyces cerevisiaeMechanistic Target of Rapamycin Complex 1Biology03 medical and health sciencesRibosomal proteinTranscription (biology)Gene Expression Regulation FungalGeneticsTranscriptional regulationBinding sitePromoter Regions GeneticTranscription factorGeneGeneticsBinding SitesTOR Serine-Threonine KinasesGene regulation Chromatin and EpigeneticsForkhead Transcription FactorsPromoterDNA-Binding Proteins030104 developmental biologyMultiprotein ComplexesTrans-ActivatorsTranscription FactorsNucleic Acids Research
researchProduct

Regulation of the hDlg/hScrib/Hugl-1 tumour suppressor complex.

2008

The proper function of the Scribble tumour suppressor complex is dependent upon the correct localisation of its components. Previously we observed dynamic relocalisation of the hDlg component under conditions of osmotic stress. We now show that the other two components of the complex, hScrib and Hugl-1 display similar patterns of expression. We demonstrate, by shRNA ablation of hScrib expression, that hDlg and Hugl-1 are in part dependent upon hScrib for their correct localization. However under conditions of osmotic stress this apparent dependency no longer exists: hDlg and Hugl-1 localise to cell membranes independently of hScrib. We also demonstrate an interaction between the three compo…

SCRIBBlotting WesternBiologylaw.inventionCell LineSmall hairpin RNADiscs Large Homolog 1 ProteinlawSyntaxinAnimalsHumansSorbitolTransport VesiclesAdaptor Proteins Signal TransducingRegulation of gene expressionQa-SNARE ProteinsTumor Suppressor ProteinsOsmolar ConcentrationSignal transducing adaptor proteinMembrane ProteinsCell BiologyTransport proteinCell biologyVesicular transport proteinCytoskeletal ProteinsProtein TransportGene Expression RegulationMultiprotein ComplexesSuppressorRNA InterferenceSignal TransductionExperimental cell research
researchProduct

Modular organization in the reductive evolution of protein-protein interaction networks

2006

Analysis of the reduction in genome size of Buchnera aphidicola from its common ancestor E. coli shows that the organization of networks into modules is the property that seems to be directly related with the evolutionary process of genome reduction.

Systems biologyComplex systemComputational biologyBiologyGenomeProtein protein interaction networkProtein–protein interactionBuchneraInteraction networkProtein Interaction MappingEscherichia coliAnimalsHumansDatabases ProteinGeneticsbusiness.industrySystems BiologyResearchbiochemical phenomena metabolism and nutritionModular designbiology.organism_classificationBiological EvolutionProtein Structure TertiaryStructural Homology ProteinMultiprotein ComplexesBuchnerabusinessAlgorithmsGenome BacterialGenome Biology
researchProduct

Common gene expression strategies revealed by genome-wide analysis in yeast

2007

A comprehensive analysis of six variables characterizing gene expression in yeast, including transcription and translation, mRNA and protein amounts, reveals a general tendency for levels of mRNA and protein to be harmonized, and for functionally related genes to have similar values for these variables.

TBX1GeneticsRegulation of gene expressionResearchRNA StabilityStructural geneGenes FungalComputational BiologyGene ExpressionSaccharomyces cerevisiaeBiologyRetinoblastoma-like protein 1EIF4EBP1SaccharomycesGene Expression Regulation FungalMultiprotein ComplexesSNAP23Gene expressionExpressió genèticaCluster AnalysisGeneGenome Biology
researchProduct

In human endothelial cells rapamycin causes mTORC2 inhibition and impairs cell viability and function.

2008

Aim Drug-eluting stents are widely used to prevent restenosis but are associated with late endothelial damage. To understand the basis for this effect, we have studied the consequences of a prolonged incubation with rapamycin on the viability and functions of endothelial cells. Methods and results Human umbilical vein or aorta endothelial cells were exposed to rapamycin in the absence or in the presence of tumour necrosis factor α (TNFα). After a 24 h-incubation, rapamycin (100 nM) caused a significant cell loss associated with the increase of both apoptosis and necrosis, as quantified by propidium iodide staining, caspase 3 activity, and lactate dehydrogenase release. Rapamycin also impair…

Time FactorsPhysiologyApoptosismTORC1Polymerase Chain Reactionchemistry.chemical_compoundCell MovementStress FibersMicroscopy ConfocalCaspase 3TOR Serine-Threonine KinasesNitric Oxide Synthase Type IIIRibosomal Protein S6 Kinases 70-kDaUp-RegulationEndothelial stem cellmedicine.anatomical_structureBiochemistryCardiology and Cardiovascular MedicineE-SelectinEndotheliumNitric Oxide Synthase Type IIICell SurvivalBlotting WesternEnzyme-Linked Immunosorbent AssayBiologyMechanistic Target of Rapamycin Complex 1Nitric OxideTacrolimusNecrosisTheophyllinePhysiology (medical)medicineHumansImmunoprecipitationViability assayPropidium iodideProtein kinase BAdaptor Proteins Signal TransducingSirolimusDose-Response Relationship DrugL-Lactate DehydrogenaseTumor Necrosis Factor-alphaEndothelial CellsProteinsCardiovascular AgentsRegulatory-Associated Protein of mTORMolecular biologyRapamycin-Insensitive Companion of mTOR ProteinchemistryMultiprotein ComplexesTOR Serine-Threonine KinasesCarrier ProteinsProtein KinasesTranscription FactorsCardiovascular research
researchProduct