Search results for "Motifs"

showing 10 items of 180 documents

Selective targeting of avidin/mannose 6-phosphate receptor chimeras to early or late endosomes

2000

Summary In this study we have used the Semliki forest virus expression system to transiently express chimeric proteins that contain transmembrane and cytoplasmic domains of the cation-independent mannose 6-phosphate receptor (CI-MPR) fused to chicken avidin. Immunofluorescence and electron microscopy studies showed that the chimeric protein with the entire cytoplasmic domain of CI-MPR was transported to late endosomes, where it accumulated. We made use of the biotin-binding capacity of lumenal avidin, and found that, in agreement with this distribution, the chimeric protein could be labelled with biotinylated HRP endocytosed for a long, but not a brief, period of time. However, truncation o…

CytoplasmTime FactorsHistologyEndosomeRecombinant Fusion ProteinsAmino Acid MotifsGreen Fluorescent ProteinsEndosomesEndocytosisReceptor IGF Type 2Pathology and Forensic Medicine03 medical and health sciencesCationsCricetinaeAnimalsBiotinylation030304 developmental biologyProtein Synthesis Inhibitors0303 health sciencesBrefeldin AMannose 6-phosphate receptorbiologyCell Membrane030302 biochemistry & molecular biologyPovidoneBiological TransportCell BiologyGeneral MedicineAvidinSilicon DioxideSemliki forest virusFusion proteinMolecular biologyEndocytosisTransmembrane proteinProtein Structure TertiaryLuminescent ProteinsMicroscopy ElectronTransmembrane domainCross-Linking ReagentsMicroscopy FluorescenceBiotinylationbiology.proteinCattleChickensDimerizationAvidinEuropean Journal of Cell Biology
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Amyloid Precursor-like Protein 1 Influences Endocytosis and Proteolytic Processing of the Amyloid Precursor Protein

2005

Ectodomain shedding of the amyloid precursor protein (APP) is a key regulatory step in the generation of the Alzheimer disease amyloid beta peptide (Abeta). The molecular mechanisms underlying the control of APP shedding remain little understood but are in part dependent on the low density lipoprotein receptor-related protein (LRP), which is involved in APP endocytosis. Here, we show that the APP homolog APLP1 (amyloid precursor-like protein 1) influences APP shedding. In human embryonic kidney 293 cells expression of APLP1 strongly activated APP shedding by alpha-secretase and slightly reduced beta-secretase cleavage. As revealed by domain deletion analysis, the increase in APP shedding re…

CytoplasmTime FactorsRecombinant Fusion ProteinsAmino Acid MotifsBlotting WesternGenetic VectorsEndocytic cycleCHO CellsTransfectionEndocytosisBiochemistryCell LineAmyloid beta-Protein PrecursorGenes ReporterCricetinaeChlorocebus aethiopsEndopeptidasesmental disordersAmyloid precursor proteinAnimalsAspartic Acid EndopeptidasesHumansImmunoprecipitationAPLP1Molecular BiologyModels GeneticbiologyChemistryHEK 293 cellsP3 peptideCell BiologyEndocytosisProtein Structure TertiaryMicroscopy FluorescenceBiochemistryAlpha secretaseEctodomainCOS Cellsbiology.proteinAmyloid Precursor Protein SecretasesPeptidesGene DeletionPlasmidsJournal of Biological Chemistry
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A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase

1999

Protein tyrosine phosphatase PTP-SL retains mitogen-activated protein (MAP) kinases in the cytoplasm in an inactive form by association through a kinase interaction motif (KIM) and tyrosine dephosphorylation. The related tyrosine phosphatases PTP-SL and STEP were phosphorylated by the cAMP-dependent protein kinase A (PKA). The PKA phosphorylation site on PTP-SL was identified as the Ser231 residue, located within the KIM. Upon phosphorylation of Ser231, PTP-SL binding and tyrosine dephosphorylation of the MAP kinases extracellular signal–regulated kinase (ERK)1/2 and p38α were impaired. Furthermore, treatment of COS-7 cells with PKA activators, or overexpression of the Cα catalytic subunit …

Cytoplasmanimal structuresRecombinant Fusion ProteinsCèl·lulesAmino Acid MotifsNerve Tissue ProteinsProtein tyrosine phosphataseSH2 domainTransfectionenvironment and public healthModels Biologicalp38 Mitogen-Activated Protein KinasesReceptor tyrosine kinaseSH3 domainCell LinePhosphoserinetyrosine phosphatasesAnimalsHumansProtein phosphorylationPKAReceptor-Like Protein Tyrosine Phosphatases Class 7PhosphorylationPTP-SLCell NucleusMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3biologyBrief ReportIntracellular Signaling Peptides and ProteinsBiological TransportCell BiologyProtein Tyrosine Phosphatases Non-ReceptorCyclic AMP-Dependent Protein KinasesEnzyme Activationenzymes and coenzymes (carbohydrates)MAP kinasesBiochemistryMitogen-activated protein kinaseCOS CellsMutationbiology.proteinPhosphorylationMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesEnzimssignal transductionProto-oncogene tyrosine-protein kinase Src
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Nuclear Localization of PTEN by a Ran-dependent Mechanism Enhances Apoptosis: Involvement of an N-Terminal Nuclear Localization Domain and Multiple N…

2006

The targeting of the tumor suppressor PTEN protein to distinct subcellular compartments is a major regulatory mechanism of PTEN function, by controlling its access to substrates and effector proteins. Here, we investigated the molecular basis and functional consequences of PTEN nuclear/cytoplasmic distribution. PTEN accumulated in the nucleus of cells treated with apoptotic stimuli. Nuclear accumulation of PTEN was enhanced by mutations targeting motifs in distinct PTEN domains, and it was dependent on an N-terminal nuclear localization domain. Coexpression of a dominant negative Ran GTPase protein blocked PTEN accumulation in the nucleus, which was also affected by coexpression of importin…

Cèl·lulesAmino Acid MotifsMolecular Sequence DataNuclear Localization SignalsApoptosisBiologyModels BiologicalCatalysislaw.inventionMicelawChlorocebus aethiopsmedicineAnimalsHumansPTENAmino Acid SequenceProteïnes supressores de tumorsMolecular BiologyCells CulturedSequence DeletionCell NucleusCOS cellsEffectorPTEN Phosphohydrolase3T3 CellsArticlesCell BiologyProtein Structure TertiaryRatsTransport proteinProtein TransportCell nucleusran GTP-Binding Proteinmedicine.anatomical_structureCOS CellsRanbiology.proteinCancer researchSuppressorNuclear localization sequenceHeLa CellsMolecular Biology of the Cell
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Role of two operators in regulating the plasmid-borne raf operon of Escherichia coli

1994

The plasmid-borne raf operon encodes functions required for the inducible uptake and utilization of raffinose in Escherichia coli K12. The expression of three structural genes for alpha-galactosidase (rafA), Raf permease (rafB) and sucrose hydrolase (rafD) is negatively controlled by the binding of RafR repressor (rafR) to two operator sites, O1 and O2, that flank the -35 sequence of the raf promoter, PA. In vitro, O1 and O2 are occupied on increasing the concentration of RafR, without detectable preference for one site or the other or any indication of cooperative binding. Nucleotide substitutions at positions 3, 4 or 5 in an operator half-site prevented repressor binding, supporting a mod…

DNA BacterialOperator Regions GeneticOperonBase pairMolecular Sequence DataRepressorBiologyBinding CompetitiveRaffinoseTranscription (biology)OperonEscherichia coliGeneticsBinding siteSite-directed mutagenesisMolecular BiologyBase SequenceHelix-Loop-Helix MotifsStructural geneCooperative bindingGene Expression Regulation BacterialDNA-Binding ProteinsRepressor ProteinsBiochemistryGenes Bacterialalpha-GalactosidaseMutagenesis Site-DirectedAutoradiographyElectrophoresis Polyacrylamide GelPlasmidsMolecular and General Genetics MGG
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Axial (apical-basal) expression of pro-apoptotic and pro-survival genes in the lake baikal demosponge Lubomirskia baicalensis.

2006

Like in all other Metazoa, also in sponges (Porifera) proliferation, differentiation, and death of cells are controlled by apoptotic processes, thus allowing the establishment of a Bauplan (body plan). The demosponge Lubomirskia baicalensis from the Lake Baikal is especially suitable to assess the role of the apoptotic molecules, since its grade of construction is highly elaborated into an encrusting base and branches composed of modules lined up along the apical-basal axis. The four cDNAs, ALG-2, BAK, MA-3, and Bcl-2, were isolated from this sponge species. The expression levels of these genes follow characteristic gradients. While the proapoptotic genes are highly expressed at the base of…

DNA ComplementaryMolecular Sequence DataGene ExpressionApoptosisFresh WaterModels BiologicalConserved sequenceRussiaDemospongePhylogeneticsGene expressionCell polarityGeneticsAnimalsAmino Acid SequenceEF Hand MotifsMolecular BiologyGeneCaspaseConserved SequencePhylogenyCaspase 8Glutathione PeroxidasebiologySequence Homology Amino AcidEcologyCaspase 3Cell PolarityCell BiologyGeneral MedicineSequence Analysis DNAbiology.organism_classificationBlotting NorthernCell biologyPoriferaProtein Structure TertiarySpongeProto-Oncogene Proteins c-bcl-2Caspasesbiology.proteinDNA and cell biology
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Structure of SNX9 SH3 in complex with a viral ligand reveals the molecular basis of its unique specificity for alanine-containing class I SH3 motifs

2021

Class I SH3 domain-binding motifs generally comply with the consensus sequence [R/K]x0PxxP, the hydrophobic residue 0 being proline or leucine. We have studied the unusual 0 = Ala-specificity of SNX9 SH3 by determining its complex structure with a peptide present in eastern equine encephalitis virus (EEEV) nsP3. The structure revealed the length and composition of the n-Src loop as important factors determining specificity. We also compared the affinities of EEEV nsP3 peptide, its mutants, and cellular ligands to SNX9 SH3. These data suggest that nsP3 has evolved to minimize reduction of conformational entropy upon binding, hence acquiring stronger affinity, enabling takeover of SNX9. The R…

DYNAMICSPROLINE-RICH PEPTIDESviruksetPROTEINSvirusesHTLV-1 GagLigandsEVOLUTIONARY CONSERVATIONalfaviruksetsrc Homology DomainsHIGH-AFFINITYretroviruksetDOMAINStructural BiologyBINDINGAnimalsHorsesMolecular Biologysoluviestintä11832 Microbiology and virologyAlanineBinding SitesPXXP MOTIFSisothermal titration calorimetrySH3solution NMR spectroscopyEEEV nsP3HIV-11182 Biochemistry cell and molecular biologyproteiinitCHEMICAL-SHIFTS3111 BiomedicinePeptidesSNX9Protein Binding
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EGFL7 ligates αvβ3 integrin to enhance vessel formation

2013

Angiogenesis, defined as blood vessel formation from a preexisting vasculature, is governed by multiple signal cascades including integrin receptors, in particular integrin αVβ3. Here we identify the endothelial cell (EC)-secreted factor epidermal growth factor-like protein 7 (EGFL7) as a novel specific ligand of integrin αVβ3, thus providing mechanistic insight into its proangiogenic actions in vitro and in vivo. Specifically, EGFL7 attaches to the extracellular matrix and by its interaction with integrin αVβ3 increases the motility of EC, which allows EC to move on a sticky underground during vessel remodeling. We provide evidence that the deregulation of EGFL7 in zebrafish embryos leads …

EGF Family of ProteinsEmbryo NonmammalianAngiogenesisAmino Acid MotifsImmunologyIntegrinGene ExpressionMice NudeEndothelial Growth FactorsBiochemistryCollagen receptorMiceCell MovementCell AdhesionHuman Umbilical Vein Endothelial CellsmedicineAnimalsHumansImmunoprecipitationPhosphorylationZebrafishbiologyReverse Transcriptase Polymerase Chain ReactionChemistryCalcium-Binding ProteinsInfarction Middle Cerebral ArteryVenous plexusCell BiologyHematologyIntegrin alphaVbeta3ImmunohistochemistryExtracellular MatrixCell biologyEndothelial stem cellHEK293 Cellsmedicine.anatomical_structureIntegrin alpha MImmunologybiology.proteinBlood VesselsRNA InterferenceIntegrin beta 6Protein BindingBlood vesselBlood
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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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γ2-Adaptin, a Ubiquitin-interacting Adaptor, Is a Substrate to Coupled Ubiquitination by the Ubiquitin Ligase Nedd4 and Functions in the Endosomal Pa…

2008

gamma2-Adaptin is a putative member of the clathrin adaptor protein family with unknown physiological function. We previously reported that gamma2-adaptin acts as a ubiquitin receptor by virtue of its ubiquitin-interacting motif. Here we demonstrate that this motif mediates a specific physical interaction with the ubiquitin ligase Nedd4 and promotes ubiquitination of gamma2-adaptin. By mapping regions of Nedd4 involved in binding to gamma2-adaptin, we identified its C2 domain to be essential, whereas the WW and HECT domains are dispensable. Consistent with this, we uncovered that the C2 domain of Nedd4 is ubiquitinated itself and as such is recruited by the ubiquitin-interacting motif of ga…

EndosomeNedd4 Ubiquitin Protein LigasesUbiquitin-Protein LigasesAmino Acid MotifsNEDD4Endosomesmacromolecular substancesUbiquitin-conjugating enzymeBiochemistryClathrinSubstrate SpecificityUbiquitinCell Line TumorHumansAdaptor Protein Complex gamma SubunitsMolecular BiologyC2 domainEndosomal Sorting Complexes Required for TransportEpidermal Growth FactorbiologyUbiquitinCell MembraneUbiquitinationSignal transducing adaptor proteinCell BiologyUbiquitin ligaseCell biologybiology.proteinProtein BindingJournal of Biological Chemistry
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