Search results for "Intracellular Signaling Peptides and Protein"

showing 10 items of 140 documents

Chromatin modifiers and recombination factors promote a telomere fold-back structure, that is lost during replicative senescence.

2020

Telomeres have the ability to adopt a lariat conformation and hence, engage in long and short distance intra-chromosome interactions. Budding yeast telomeres were proposed to fold back into subtelomeric regions, but a robust assay to quantitatively characterize this structure has been lacking. Therefore, it is not well understood how the interactions between telomeres and non-telomeric regions are established and regulated. We employ a telomere chromosome conformation capture (Telo-3C) approach to directly analyze telomere folding and its maintenance in S. cerevisiae. We identify the histone modifiers Sir2, Sin3 and Set2 as critical regulators for telomere folding, which suggests that a dis…

TelomeraseProtein Folding:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::DNA-Binding Proteins::Rad52 DNA Repair and Recombination Protein [Medical Subject Headings]:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Fungal Proteins::Saccharomyces cerevisiae Proteins [Medical Subject Headings]Gene ExpressionYeast and Fungal ModelsArtificial Gene Amplification and ExtensionQH426-470BiochemistryPolymerase Chain ReactionChromosome conformation captureHistonesCromatina0302 clinical medicineSirtuin 2Macromolecular Structure AnalysisSilent Information Regulator Proteins Saccharomyces cerevisiaeCellular Senescence:Organisms::Eukaryota::Fungi::Yeasts::Saccharomyces::Saccharomyces cerevisiae [Medical Subject Headings]0303 health sciencesChromosome BiologyEukaryota:Phenomena and Processes::Genetic Phenomena::Genetic Processes::DNA Replication [Medical Subject Headings]TelomereSubtelomere:Anatomy::Cells::Cellular Structures::Intracellular Space::Cell Nucleus::Cell Nucleus Structures::Intranuclear Space::Chromosomes::Chromosome Structures::Telomere [Medical Subject Headings]Chromatin3. Good healthChromatinCell biologyNucleic acidsTelomeres:Phenomena and Processes::Cell Physiological Phenomena::Cell Physiological Processes::Cell Cycle::Cell Division::Telomere Homeostasis [Medical Subject Headings]Experimental Organism SystemsDaño del ADNEpigeneticsResearch ArticleSenescenceDNA Replication:Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Hydrolases::Amidohydrolases::Histone Deacetylases [Medical Subject Headings]Chromosome Structure and FunctionProtein StructureSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeBiologyResearch and Analysis MethodsHistone DeacetylasesChromosomes03 medical and health sciencesSaccharomycesModel Organisms:Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Transferases::One-Carbon Group Transferases::Methyltransferases [Medical Subject Headings]:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Intracellular Signaling Peptides and Proteins::Sirtuins::Sirtuin 2 [Medical Subject Headings]:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Fungal Proteins::Saccharomyces cerevisiae Proteins::Silent Information Regulator Proteins Saccharomyces cerevisiae [Medical Subject Headings]DNA-binding proteinsGenetics:Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Recombinases::Rec A Recombinases::Rad51 Recombinase [Medical Subject Headings]Molecular Biology TechniquesMolecular Biology030304 developmental biologyCromosomasSenescencia celularOrganismsFungiBiology and Life SciencesProteinsTelomere HomeostasisCell BiologyDNAMethyltransferasesG2-M DNA damage checkpointProteína recombinante y reparadora de ADN Rad52YeastTelomereRad52 DNA Repair and Recombination ProteinRepressor ProteinsAnimal Studies:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Transcription Factors::Repressor Proteins [Medical Subject Headings]DNA damageRad51 RecombinaseHomologous recombination030217 neurology & neurosurgeryTelómeroDNA DamagePLoS Genetics
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The tumor suppressor CYLD controls the function of murine regulatory T cells.

2012

Abstract CYLD was originally identified as a tumor suppressor gene mutated in familial cylindromatosis, an autosomal dominant predisposition to multiple benign neoplasms of the skin known as cylindromas. The CYLD protein is a deubiquitinating enzyme that acts as a negative regulator of NF-κB and JNK signaling through its interaction with NEMO and TNFR-associated factor 2. We have previously described a novel mouse strain that expresses solely and excessively a naturally occurring splice variant of CYLD (CYLDex7/8). In this study, we demonstrate that CYLD plays a critical role in Treg development and function. T cells of CYLDex7/8 mice had a hyperactive phenotype manifested by increased prod…

Tumor suppressor geneT cellImmunologyBiologyT-Lymphocytes RegulatoryDeubiquitinating Enzyme CYLDlaw.inventionProinflammatory cytokineMicelawmedicineImmunology and AllergyAnimalsCTLA-4 AntigenIL-2 receptorTumor Suppressor ProteinsInterleukin-2 Receptor alpha SubunitIntracellular Signaling Peptides and ProteinsNF-kappa BFOXP3PhenotypeMice Mutant StrainsCell biologyDeubiquitinating Enzyme CYLDCysteine Endopeptidasesmedicine.anatomical_structureGene Expression RegulationImmunologySuppressorJournal of immunology (Baltimore, Md. : 1950)
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LaXp180, a mammalian ActA-binding protein, identified with the yeast two-hybrid system, co-localizes with intracellular Listeria monocytogenes

2001

The Listeria monocytogenes surface protein ActA is an important virulence factor required for listerial intracellular movement by inducing actin polymerization. The only host cell protein known that directly interacts with ActA is the phosphoprotein VASP, which binds to the central proline-rich repeat region of ActA. To identify additional ActA-binding proteins, we applied the yeast two-hybrid system to search for mouse proteins that interact with ActA. A mouse cDNA library was screened for ActA-interacting proteins (AIPs) using ActA from strain L. monocytogenes EGD as bait. Three different AIPs were identified, one of which was identical to the human protein LaXp180 (also called CC1). Bind…

Two-hybrid screeningImmunologyMolecular Sequence DataAutophagy-Related ProteinsFluorescent Antibody TechniqueStathminmacromolecular substancesmedicine.disease_causeMicrobiologylaw.inventionCell LineMicefluids and secretionsListeria monocytogenesBacterial ProteinslawVirologyTwo-Hybrid System TechniquesmedicineAnimalsHumansListeriosisAmino Acid SequencebiologyReverse Transcriptase Polymerase Chain ReactionBinding proteintechnology industry and agricultureIntracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsListeria monocytogenesActinsBiochemistryPhosphoproteinembryonic structuresCOS CellsRecombinant DNAbiology.proteinbacteriaSignal transductionCarrier ProteinsIntracellularPlasmids
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The 3'-UTR of the mRNA coding for the major protein kinase C substrate MARCKS contains a novel CU-rich element interacting with the mRNA stabilizing …

2003

The expression of the major protein kinase C substrate MARCKS (myristoylated alanine-rich C kinase substrate) is controlled by the stability of its mRNA. While the MARCKS mRNA is long living in quiescent fibroblasts (t1/2 = 14 h), its half-life time is drastically reduced (t1/2 = 2 h) in cells treated with phorbol esters to activate protein kinase C (PKC) or treated with growth factors. In a first step to study the underlying mechanism we identified both a cis-element on the MARCKS mRNA and the corresponding trans-acting factors. Fusing the complete 3'-UTR or specific regions of the 3'-UTR of the MARCKS gene to a luciferase reporter gene caused a drastic decrease in luciferase expression to…

Untranslated regionRecombinant Fusion ProteinsELAV-Like Protein 1Down-RegulationNerve Tissue ProteinsELAV-Like Protein 4BiologyBiochemistryELAV-Like Protein 1MiceGenes ReporterAnimalsRNA MessengerMARCKSLuciferasesMyristoylated Alanine-Rich C Kinase Substrate3' Untranslated RegionsProtein Kinase CProtein kinase CAU-rich elementMessenger RNAThree prime untranslated regionIntracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsRNA-Binding Proteins3T3 CellsFibroblastsMolecular biologyELAV ProteinsAntigens SurfaceMARCKS GeneEuropean Journal of Biochemistry
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Intraflagellar transport protein 172 is essential for primary cilia formation and plays a vital role in patterning the mammalian brain

2008

AbstractIFT172, also known as Selective Lim-domain Binding protein (SLB), is a component of the intraflagellar transport (IFT) complex. In order to evaluate the biological role of the Ift172 gene, we generated a loss-of-function mutation in the mouse. The resulting Slb mutant embryos die between E12.5 and 13.0, and exhibit severe cranio-facial malformations, failure to close the cranial neural tube, holoprosencephaly, heart edema and extensive hemorrhages. Cilia outgrowth in cells of the neuroepithelium is initiated but the axonemes are severely truncated and do not contain visible microtubules. Morphological and molecular analyses revealed a global brain-patterning defect along the dorsal–…

animal structuresBody PatterningNodal ProteinSlbNodalBiologyArticleMiceFGF8Intraflagellar transportHoloprosencephalymedicineMHB boundaryAnimalsHedgehog ProteinsRNA MessengerCiliaNodeMolecular BiologyAdaptor Proteins Signal TransducingBody PatterningGeneticsMammalsCell DeathCiliumEndodermNeural tubeIntracellular Signaling Peptides and ProteinsBrainGene Expression Regulation DevelopmentalCell BiologyEmbryo MammalianCell biologyNeuroepithelial cellGastrulationCytoskeletal Proteinsmedicine.anatomical_structurePhenotypeIFT172Gene Targetingembryonic structuresNODALBiomarkersGene DeletionDevelopmental BiologySignal TransductionDevelopmental Biology
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TAZ is required for metastatic activity and chemoresistance of breast cancer stem cells

2015

Metastatic growth in breast cancer (BC) has been proposed as an exclusive property of cancer stem cells (CSCs). However, formal proof of their identity as cells of origin of recurrences at distant sites and the molecular events that may contribute to tumor cell dissemination and metastasis development are yet to be elucidated. In this study, we analyzed a set of patient-derived breast cancer stem cell (BCSC) lines. We found that in vitro BCSCs exhibit a higher chemoresistance and migratory potential when compared with differentiated, nontumorigenic, breast cancer cells (dBCCs). By developing an in vivo metastatic model simulating the disease of patients with early BC, we observed that BCSCs…

cancer stem cellsTAZAnimals; Biomarkers Tumor; Breast Neoplasms; Cell Line Tumor; Disease-Free Survival; Female; Gene Expression Regulation Neoplastic; Humans; Mice; Neoplasm Metastasis; Neoplasm Recurrence Local; Neoplastic Stem Cells; Transcription Factors; Xenograft Model Antitumor AssaysCancer ResearchBioinformaticschemotherapyMetastasistaz; breast cancerMiceNeoplasm Metastasiseducation.field_of_studyTumorIntracellular Signaling Peptides and ProteinsCell cycleGene Expression Regulation NeoplasticLocalNeoplastic Stem Cellsbreast cancer; cancer stem cells; chemotherapy; metastasis; TAZ; Animals; Biomarkers Tumor; Breast Neoplasms; Cell Line Tumor; Disease-Free Survival; Female; Gene Expression Regulation Neoplastic; Humans; Intracellular Signaling Peptides and Proteins; Mice; Neoplasm Metastasis; Neoplasm Recurrence Local; Neoplastic Stem Cells; Xenograft Model Antitumor Assays; Molecular Biology; Genetics; Cancer ResearchFemaleStem cellPopulationBreast NeoplasmsBiologyDisease-Free SurvivalCell Linebreast cancer cancer stem cells TAZBreast cancerbreast cancerCancer stem cellSettore MED/04 - PATOLOGIA GENERALECell Line TumormedicineBiomarkers TumorGeneticsmetastasisAnimalsHumanseducationMolecular BiologyHippo signaling pathwayNeoplasticCancermedicine.diseaseXenograft Model Antitumor AssaysNeoplasm RecurrenceGene Expression RegulationTranscriptional Coactivator with PDZ-Binding Motif ProteinsCancer researchTrans-ActivatorsNeoplasm Recurrence LocalBiomarkersTranscription Factors
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The Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) is Sequentially Phosphorylated by Conventional, Novel and Atypical Isotypes of Protein Kin…

1995

The myristoylated alanine-rich C-kinase substrate (MARCKS) is the major protein kinase C (PKC) substrate in many cell types including fibroblasts and brain cells. Here we describe the phosphorylation of MARCKS and the site specificity for different PKC isotypes. Conventional (c)PKC beta 1, novel (n)PKC delta and nPKC epsilon efficiently phosphorylated the MARCKS protein in vitro. The Km values were extremely low, reflecting a high affinity between kinases and substrate. The apparent affinity of nPKC delta (Km = 0.06 microM) was higher than that of nPKC epsilon and cPKC beta 1 (Km = 0.32 microM). The rate of substrate phosphorylation was inversely correlated with affinity and decreased in th…

inorganic chemicalsKinaseChemistryIntracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsContext (language use)macromolecular substancesenvironment and public healthBiochemistryMolecular biologyCell biologyIsoenzymesSerineKineticsenzymes and coenzymes (carbohydrates)Substrate-level phosphorylationbacteriaPhosphorylationPhosphorylationMARCKSMyristoylated Alanine-Rich C Kinase SubstrateProtein Kinase CProtein kinase CMyristoylationEuropean Journal of Biochemistry
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Inhibition of Delta-like 4 mediated signaling induces abortion in mice due to deregulation of decidual angiogenesis.

2013

Objective: To explore whether the Dll4/Notch1 pathway plays a key role in regulating the vascular endothelial growth factor (VEGF)/VEGF receptor 2 (VEGFR2) driven decidual angiogenesis and related pregnancy through induction of a tip/stalk phenotype. Methods: Progesterone-replaced ovariectomized pregnant mice received a single injection of YW152F (Dll4 blocking antibody, BAb) or placebo at embryonic day (E) 4.5. Animals were sacrificed at different time points; blood and uterus were collected for further analysis. Number of embryos and implantation site, uteri weight, and serum progesterone levels were assessed. Alterations in the tip/stalk phenotype were determined by quantitative immunofl…

medicine.medical_specialtyAngiogenesisNotch pathwayNotch signaling pathwayUterusEmbryonic DevelopmentNeovascularization PhysiologicApoptosisGestational AgeDll4BiologyPregnancy disruptionAndrologychemistry.chemical_compoundMicePregnancyInternal medicinemedicineDeciduaAnimalsAntibodies BlockingAdaptor Proteins Signal TransducingCell ProliferationCell growthDeciduaCalcium-Binding ProteinsIntracellular Signaling Peptides and ProteinsObstetrics and GynecologyMembrane ProteinsEmbryoVEGFVascular Endothelial Growth Factor Receptor-2Vascular endothelial growth factorDisease Models Animalmedicine.anatomical_structureEndocrinologyReproductive MedicinechemistryApoptosiscardiovascular systemEmbryo LossFemaleAngiogenesisDevelopmental BiologySignal TransductionPlacenta
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Antiapoptotic effect of calcitonin gene-related peptide on oxidative stress-induced injury in H9c2 cardiomyocytes via the RAMP1/CRLR complex.

2005

Calcitonin gene-related peptide (CGRP) plays an important role in the mediation of protective effects observed in situations such as ischemic preconditioning in rat hearts. In this study, we investigated in H9c2 rat cardiomyoblasts if the protective effect of CGRP could be linked to an inhibitory effect on the apoptotic pathway. We also determined the specificity of observed effects by treatment with adrenomedullin (ADM) in stress conditions generated by 100 microM hydrogen peroxide. Using MTT assays, we demonstrate that a pretreatment with CGRP decreases by half the loss of cell viability induced by H(2)O(2). CGRP inhibits phosphatidylserine externalization, caspase 3 activation and DNA fr…

medicine.medical_specialtyCalcitonin Gene-Related PeptideCaspase 3DNA FragmentationCalcitonin gene-related peptideReceptor Activity-Modifying Protein 2Receptor Activity-Modifying Protein 3Receptor Activity-Modifying ProteinsCell LineReceptor Activity-Modifying Protein 1Internal medicinemedicineAnimalsMyocytes CardiacViability assayMolecular BiologyReceptor activity-modifying proteinintegumentary systemChemistryCalcitonin Receptor-Like ProteinIntracellular Signaling Peptides and ProteinsMembrane ProteinsReceptors CalcitoninPeptide FragmentsRatsAdrenomedullinOxidative StressEndocrinologyGene Expression RegulationRAMP2ApoptosisRAMP1Multiprotein ComplexesIschemic Preconditioning MyocardialCardiology and Cardiovascular MedicineMioticsSignal TransductionJournal of molecular and cellular cardiology
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Nuclear localization but not PML protein is required for incorporation of the papillomavirus minor capsid protein L2 into virus-like particles.

2004

ABSTRACT Recent reports suggest that nuclear domain(s) 10 (ND10) is the site of papillomavirus morphogenesis. The viral genome replicates in or close to ND10. In addition, the minor capsid protein, L2, accumulates in these subnuclear structures and recruits the major capsid protein, L1. We have now used cell lines deficient for promyelocytic leukemia (PML) protein, the main structural component of ND10, to study the role of this nuclear protein for L2 incorporation into virus-like particles (VLPs). L2 expressed in PML protein knockout (PML −/− ) cells accumulated in nuclear dots, which resemble L2 aggregates forming at ND10 in PML protein-containing cells. These L2 assemblies also attracted…

virusesImmunologyActive Transport Cell NucleusNuclear dotsBiologyPromyelocytic Leukemia ProteinMicrobiologyCell LinePromyelocytic leukemia proteinMiceDeath-associated protein 6Virus-like particleVirologymedicineAnimalsHumansNuclear proteinPapillomaviridaeAdaptor Proteins Signal TransducingCell NucleusTumor Suppressor ProteinsStructure and AssemblyIntracellular Signaling Peptides and ProteinsVirionvirus diseasesNuclear ProteinsOncogene Proteins Viralbiochemical phenomena metabolism and nutritionMolecular biologyCell biologyNeoplasm ProteinsCell nucleusMicroscopy Electronmedicine.anatomical_structureInsect ScienceMutationbiology.proteinCapsid ProteinsNuclear transportCarrier ProteinsCo-Repressor ProteinsNuclear localization sequenceMolecular ChaperonesTranscription FactorsJournal of virology
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