Search results for "Interaction domains"

showing 10 items of 46 documents

Identification of the integrin-binding site on coagulation factor VIIa required for proangiogenic PAR2 signaling.

2018

The tissue factor (TF) pathway serves both hemostasis and cell signaling, but how cells control these divergent functions of TF remains incompletely understood. TF is the receptor and scaffold of coagulation proteases cleaving protease-activated receptor 2 (PAR2) that plays pivotal roles in angiogenesis and tumor development. Here we demonstrate that coagulation factor VIIa (FVIIa) elicits TF cytoplasmic domain-dependent proangiogenic cell signaling independent of the alternative PAR2 activator matriptase. We identify a Lys-Gly-Glu (KGE) integrin-binding motif in the FVIIa protease domain that is required for association of the TF-FVIIa complex with the active conformer of integrin β1. A po…

0301 basic medicineCell signalingImmunologyIntegrinNeovascularization PhysiologicFactor VIIa030204 cardiovascular system & hematologyBiochemistryThromboplastinThrombosis and Hemostasis03 medical and health sciencesTissue factorMice0302 clinical medicineAnimalsHumansReceptor PAR-2Protein Interaction Domains and MotifsProtein Interaction MapsProtein kinase ACells CulturedIntegrin bindingBinding SitesbiologyChemistryIntegrin beta1Cell BiologyHematologyCell biologyCrosstalk (biology)030104 developmental biologyADP-Ribosylation Factor 6biology.proteinNIH 3T3 CellsPhosphorylationSignal transductionProtein BindingSignal TransductionBlood
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Evolutionary conserved role of eukaryotic translation factor eIF5A in the regulation of actin-nucleating formins

2017

AbstractElongation factor eIF5A is required for the translation of consecutive prolines, and was shown in yeast to translate polyproline-containing Bni1, an actin-nucleating formin required for polarized growth during mating. Here we show that Drosophila eIF5A can functionally replace yeast eIF5A and is required for actin-rich cable assembly during embryonic dorsal closure (DC). Furthermore, Diaphanous, the formin involved in actin dynamics during DC, is regulated by and mediates eIF5A effects. Finally, eIF5A controls cell migration and regulates Diaphanous levels also in mammalian cells. Our results uncover an evolutionary conserved role of eIF5A regulating cytoskeleton-dependent processes…

0301 basic medicineFluorescent Antibody Techniquelcsh:Medicinemacromolecular substancesBiologyArticleMiceEukaryotic cells03 medical and health sciencesEukaryotic translationCell MovementPeptide Initiation FactorsCitosqueletProtein biosynthesisAnimalsProtein Interaction Domains and Motifslcsh:ScienceCytoskeletonActinMultidisciplinaryCèl·lules eucariotesMicrofilament Proteinsfungilcsh:RGene Expression Regulation DevelopmentalRNA-Binding ProteinsTranslation (biology)Biological EvolutionActinsDorsal closureCell biologyElongation factor030104 developmental biologyProtein BiosynthesisForminsMutationbiology.proteinDrosophilalcsh:QEIF5AScientific Reports
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The malate sensing two-component system MaeKR is a non-canonical class of sensory complex for C4-dicarboxylates

2017

16 páginas, 7 figuras, 2 tablas

0301 basic medicineModels MolecularAdenosine Triphosphate / metabolismProtein ConformationScienceMalatesBacterial proteins/chemistry/metabolism/geneticsPlasma protein bindingBiologyModels BiologicalArticleConserved sequence03 medical and health sciencesAdenosine TriphosphateBacterial ProteinsAdenosine Triphosphate / chemistryDicarboxylic AcidsProtein Interaction Domains and MotifsAmino Acid SequenceKinase activityPhosphorylationLactobacilus cassei/classification/physiologyMalates/metabolismPromoter Regions GeneticConserved SequencePhylogenyMultidisciplinaryQAutophosphorylationfungiRTwo-component regulatory systemResponse regulatorLacticaseibacillus casei030104 developmental biologyBiochemistryMedicineModelsbiologica/moleculPhosphorylationCconserved secuenceProtein MultimerizationBinding domainProtein BindingScientific Reports
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Sensory domain contraction in histidine kinase CitA triggers transmembrane signaling in the membrane-bound sensor

2017

Bacteria use membrane-integral sensor histidine kinases (HK) to perceive stimuli and transduce signals from the environment to the cytosol. Information on how the signal is transmitted across the membrane by HKs is still scarce. Combining both liquid- and solid-state NMR, we demonstrate that structural rearrangements in the extracytoplasmic, citrate-sensing Per-Arnt-Sim (PAS) domain of HK CitA are identical for the isolated domain in solution and in a longer construct containing the membrane-embedded HK and lacking only the kinase core. We show that upon citrate binding, the PAS domain contracts, resulting in a shortening of the C-terminal β-strand. We demonstrate that this contraction of t…

0301 basic medicineModels MolecularHistidine Kinase030106 microbiologyMolecular ConformationCitric Acid03 medical and health sciencesStructure-Activity RelationshipBacterial ProteinsPAS domainProtein Interaction Domains and MotifsAmino Acid SequenceHistidineMultidisciplinaryChemistryKinaseHistidine kinaseGeobacillusMembrane ProteinsBiological SciencesTransmembrane proteinCell biologyCytosolHelixSignal transductionProtein BindingSignal Transduction
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rbFOX1/MBNL1 competition for CCUG RNA repeats binding contributes to myotonic dystrophy type 1/type 2 differences

2018

Myotonic dystrophy type 1 and type 2 (DM1, DM2) are caused by expansions of CTG and CCTG repeats, respectively. RNAs containing expanded CUG or CCUG repeats interfere with the metabolism of other RNAs through titration of the Muscleblind-like (MBNL) RNA binding proteins. DM2 follows a more favorable clinical course than DM1, suggesting that specific modifiers may modulate DM severity. Here, we report that the rbFOX1 RNA binding protein binds to expanded CCUG RNA repeats, but not to expanded CUG RNA repeats. Interestingly, rbFOX1 competes with MBNL1 for binding to CCUG expanded repeats and overexpression of rbFOX1 partly releases MBNL1 from sequestration within CCUG RNA foci in DM2 muscle ce…

0301 basic medicineModels MolecularProtein Conformation alpha-Helical[SDV]Life Sciences [q-bio]General Physics and AstronomyGene ExpressionRNA-binding proteinCrystallography X-Raychemistry.chemical_compoundMOLECULAR-BASISGene expressionMBNL1Myotonic DystrophyComputingMilieux_MISCELLANEOUSMultidisciplinaryCHLORIDE CHANNELQRNA-Binding ProteinsRecombinant Proteins3. Good healthCell biologyCONGENITAL HEART-DISEASEDrosophila melanogasterThermodynamicsSKELETAL-MUSCLERNA Splicing FactorsCUG REPEATSProtein BindingRNA Splicing Factorsmusculoskeletal diseasesSTEADY-STATEcongenital hereditary and neonatal diseases and abnormalitiesScienceRBFOX1BiologyMyotonic dystrophyBinding CompetitiveGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesmedicineEscherichia coliAnimalsHumansProtein Interaction Domains and MotifsBinding siteNucleotide MotifsMuscle SkeletalSPLICING REGULATOR RBFOX2MUSCLEBLIND PROTEINSBinding SitesPRE-MESSENGER-RNARNAGeneral Chemistrymedicine.diseaseDisease Models AnimalKinetics030104 developmental biologychemistryTRIPLET REPEATRNAProtein Conformation beta-Strand3111 Biomedicine
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Insights into the inhibited form of the redox-sensitive SufE-like sulfur acceptor CsdE

2017

17 p.-8 fig.

0301 basic medicineProtein ConformationDimerlcsh:MedicineMolecular DynamicsCrystallography X-RayPhysical ChemistryBiochemistryDEAD-box RNA HelicasesMolecular dynamicschemistry.chemical_compoundComputational ChemistryNucleophileBiochemical Simulationslcsh:ScienceMultidisciplinaryCrystallographyChemistryOrganic CompoundsPhysicsEscherichia coli ProteinsCondensed Matter Physics3. Good healthPhysical sciencesChemistryCarbon-Sulfur LyasesBiochemistryCrystal StructureResearch ArticleChemical ElementsProtein subunitChemical physicschemistry.chemical_elementOxidative phosphorylationMolecular Dynamics Simulation03 medical and health sciencesThiolsEscherichia coliSolid State PhysicsProtein Interaction Domains and MotifsChemical BondingOrganic Chemistrylcsh:RChemical CompoundsBiology and Life SciencesComputational BiologyDimers (Chemical physics)Hydrogen BondingCell BiologySulfurAcceptorRedox sensitiveOxidative Stress030104 developmental biologyBiophysicslcsh:QProtein MultimerizationSulfur
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Identification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family

2017

AbstractWe introduce LytU, a short member of the lysostaphin family of zinc-dependent pentaglycine endopeptidases. It is a potential antimicrobial agent for S. aureus infections and its gene transcription is highly upregulated upon antibiotic treatments along with other genes involved in cell wall synthesis. We found this enzyme to be responsible for the opening of the cell wall peptidoglycan layer during cell divisions in S. aureus. LytU is anchored in the plasma membrane with the active part residing in the periplasmic space. It has a unique Ile/Lys insertion at position 151 that resides in the catalytic site-neighbouring loop and is vital for the enzymatic activity but not affecting the …

0301 basic medicineentsyymitantimicrobial compoundsPROTEINchemistry.chemical_compoundCatalytic DomainCELL-WALLBINDINGMultidisciplinaryACTIVE-SITEQRESISTANT STAPHYLOCOCCUS-AUREUSRHydrogen-Ion ConcentrationAnti-Bacterial AgentsZincBiochemistryMedicineHISTIDINESProtein BindingStaphylococcus aureusScienceenzymesBiologyCleavage (embryo)metalloproteinasesArticleCofactorBACILLUS-SUBTILISCell wallStructure-Activity Relationship03 medical and health sciencesEndopeptidasesProtein Interaction Domains and MotifsAmino Acid Sequencestaphylococciantimikrobiset yhdisteetBinding SitesLysostaphinCell MembraneActive siteIsothermal titration calorimetryPeriplasmic spaceVANCOMYCINstafylokokitmetalloproteinaasitMODEL030104 developmental biologyRESOLUTIONchemistryMutationProteolysisLysostaphinbiology.protein1182 Biochemistry cell and molecular biologyPeptidoglycanScientific Reports
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Mammary-derived growth inhibitor (MDGI) interacts with integrin α-subunits and suppresses integrin activity and invasion

2010

The majority of mortality associated with cancer is due to formation of metastases from the primary tumor. Adhesion mediated by different integrin heterodimers has an important role during cell migration and invasion. Protein interactions with the β1-integrin cytoplasmic tail are known to influence integrin affinity for extracellular ligands, but regulating binding partners for the α-subunit cytoplasmic tails have remained elusive. In this study, we show that mammary-derived growth inhibitor (MDGI) (also known as FABP-3 or H-FABP) binds directly to the cytoplasmic tail of integrin α-subunits and its expression inhibits integrin activity. In breast cancer cell lines, MDGI expression correlat…

Cancer Researchmedicine.disease_causemigrationCD49cCollagen receptor0302 clinical medicineCell Movement0303 health sciencesCell migrationMiddle Agedinvasion3. Good healthCell biologyExtracellular MatrixadhesionIntegrin alpha MMDGI030220 oncology & carcinogenesis/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingIntegrin beta 6FemaleFatty Acid Binding Protein 3Integrin alpha Chainsmedicine.medical_specialtyintegrinIntegrinMolecular Sequence DataBreast NeoplasmsBiologyFatty Acid-Binding ProteinsCollagen Type IDisease-Free Survival03 medical and health sciencesbreast cancerSDG 3 - Good Health and Well-beingInternal medicineCell Line TumorGeneticsmedicineHumansNeoplasm InvasivenessProtein Interaction Domains and MotifsAmino Acid SequenceMolecular Biology030304 developmental biologyFibronectinsFibronectinEndocrinologybiology.proteinCarcinogenesisOncogene
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The Biosynthesis of Rare Homo-Amino Acid Containing Variants of Microcystin by a Benthic Cyanobacterium

2019

Microcystins are a family of chemically diverse hepatotoxins produced by distantly related cyanobacteria and are potent inhibitors of eukaryotic protein phosphatases 1 and 2A. Here we provide evidence for the biosynthesis of rare variants of microcystin that contain a selection of homo-amino acids by the benthic cyanobacterium Phormidium sp. LP904c. This strain produces at least 16 microcystin chemical variants many of which contain homophenylalanine or homotyrosine. We retrieved the complete 54.2 kb microcystin (mcy) gene cluster from a draft genome assembly. Analysis of the substrate specificity of McyB1 and McyC adenylation domain binding pockets revealed divergent substrate specificity …

CyanobacteriamassaspektrometriaMicrocystinstoksiinitPharmaceutical ScienceMicrocystinPlanktothrixcyanobacteriaArticlebiosynteesi03 medical and health scienceschemistry.chemical_compoundBiosynthesisBacterial ProteinsDrug DiscoveryGene clusterpolycyclic compoundspolyketide synthase (PKS)Protein Interaction Domains and MotifsAmino Acid SequenceAmino AcidssyanobakteeritPharmacology Toxicology and Pharmaceutics (miscellaneous)Genelcsh:QH301-705.5Phylogeny030304 developmental biologymass spectrometrychemistry.chemical_classification0303 health sciencesbiology030302 biochemistry & molecular biologyta1182Sequence Analysis DNAbiology.organism_classificationAmino acidEnzymechemistryBiochemistrylcsh:Biology (General)adenylation domainGenes BacterialMultigene Familynonribosomal peptide synthetase (NRPS)hepatotoxinMarine Drugs
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Bending-Shear interaction domains for externally prestressed concrete girders

2013

In prestressed concrete structures, the evaluation of the safety level is generally carried out by separating the bending moment strength and the shear force capacity. Actually interaction between bending moment (M) and shear force (V) can have significant consequences on evaluations in service life, especially when the ultimate limit state (ULS) is considered. In this paper, the M-V interaction is addressed for prestressed concrete girders, in the cases of both bonded and unbonded prestressing tendons. It can be demonstrated, by drawing the interaction domains (M-V), that a significant reduction of the safety level has to be considered when shear force is evaluated together with bending mo…

EngineeringArticle SubjectShear forcebending moment-shear interaction; limit state; strength domain; external prestressing; box girderexternal prestressingshearlimit statelaw.inventionPrestressed concretelawGirderInteraction domains; bending; shear; prestressingLimit state designGeotechnical engineeringShear and moment diagramCivil and Structural Engineeringstrength domainbusiness.industrybox girderStructural engineeringbendingStress fieldSettore ICAR/09 - Tecnica Delle CostruzioniShear (geology)lcsh:TA1-2040Bending momentprestressingInteraction domainlcsh:Engineering (General). Civil engineering (General)businessbending moment-shear interaction
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