Search results for "Protein Transport"

showing 7 items of 197 documents

The closure of Pak1-dependent macropinosomes requires the phosphorylation of CtBP1/BARS

2007

Membrane fission is an essential process in membrane trafficking and other cellular functions. While many fissioning and trafficking steps are mediated by the large GTPase dynamin, some fission events are dynamin independent and involve C-terminal-binding protein-1/brefeldinA-ADP ribosylated substrate (CtBP1/BARS). To gain an insight into the molecular mechanisms of CtBP1/BARS in fission, we have studied the role of this protein in macropinocytosis, a dynamin-independent endocytic pathway that can be synchronously activated by growth factors. Here, we show that upon activation of the epidermal growth factor receptor, CtBP1/BARS is (a) translocated to the macropinocytic cup and its surroundi…

genetic structuresEndocytic cycleGTPaseBiologyTRANSCRIPTIONAL COREPRESSOREPIDERMAL GROWTH-FACTORArticleGeneral Biochemistry Genetics and Molecular BiologySYNAPTIC VESICLE ENDOCYTOSISMembrane fissionCell Line TumorMacropinocytic cupHumansPhosphorylationMacropinosomeMolecular BiologyDynaminEpidermal Growth FactorGeneral Immunology and MicrobiologyMEMBRANE FISSIONGeneral NeuroscienceActinsEnterovirus B HumanProtein Structure TertiaryTransport proteinCell biologyDNA-Binding ProteinsAlcohol OxidoreductasesProtein Transportp21-Activated KinasesPLASMA-MEMBRANEPinocytosisPhosphorylationCell Surface ExtensionsIntegrin alpha2beta1The EMBO Journal
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AMPA Receptor Auxiliary Proteins of the CKAMP Family

2019

α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors are assembled of four core subunits and several additional interacting proteins. Cystine-knot AMPA receptor-modulating proteins (CKAMPs) constitute a family of four proteins that influence the trafficking, subcellular localization and function of AMPA receptors. The four CKAMP family members CKAMP39/shisa8, CKAMP44/shisa9, CKAMP52/shisa6 and CKAMP59/shisa7 differ in their expression profile and their modulatory influence on AMPA receptor function. In this review, I report about recent findings on the differential roles of CKAMP family members.

glutamate receptorhippocampusGene ExpressionReviewAMPA receptorBiologySynaptic TransmissionCatalysisCell Linelcsh:ChemistryInorganic ChemistryLong term plasticitylateral geniculate nucleusAnimalsHumansAmino Acid SequenceReceptors AMPAAMPA receptorPhysical and Theoretical Chemistrysynaptic functionReceptorlcsh:QH301-705.5Molecular BiologySpectroscopyNeuronal Plasticitymusculoskeletal neural and ocular physiologyOrganic ChemistryGlutamate receptorGeniculate BodiesGeneral MedicineSubcellular localizationlong-term plasticityComputer Science ApplicationsCell biologyProtein TransportSynaptic functionlcsh:Biology (General)lcsh:QD1-999nervous systemauxiliary subunitMultigene FamilySynapsesCarrier ProteinsIon Channel Gatingshort-term plasticityFunction (biology)Protein BindingInternational Journal of Molecular Sciences
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Differential VASP phosphorylation controls remodeling of the actin cytoskeleton

2009

Proteins of the Enabled/vasodilator-stimulated phosphoprotein (Ena/VASP) family link signal transduction pathways to actin cytoskeleton dynamics. VASP is substrate of cAMP-dependent, cGMP-dependent and AMP-activated protein kinases that primarily phosphorylate the sites S157, S239 and T278, respectively. Here, we systematically analyzed functions of VASP phosphorylation patterns for actin assembly and subcellular targeting in vivo and compared the phosphorylation effects of Ena/VASP family members. Methods used were the reconstitution of VASP-null cells with `locked' phosphomimetic VASP mutants, actin polymerization of VASP mutants in vitro and in living cells, site-specific kinase-mediated…

macromolecular substancesBiologyCell LineMiceAnimalsHumansPhosphorylationCytoskeletonCytoskeletonActinMice KnockoutKinaseMicrofilament ProteinsEna/Vasp homology proteinsActin remodelingCell BiologyPhosphoproteinsActin cytoskeletonActinsCell biologyMice Inbred C57BLProtein TransportPhosphoproteinPhosphorylationCell Adhesion MoleculesResearch ArticleJournal of Cell Science
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Erythrocyte-associated apolipoprotein B and its relationship with clinical and subclinical atherosclerosis

2011

Eur J Clin Invest 2012; 42 (4): 365–370 Abstract Background  Apolipoprotein (apo) B-containing lipoproteins are closely linked to atherogenesis. These lipoproteins are transported in plasma and are also associated with blood leucocytes. Our aim was to investigate whether apoB-containing lipoproteins are also present on the surface of erythrocytes and investigate the relationship with the presence of atherosclerosis in a cross-sectional study. Materials and methods  Erythrocyte-bound apoB (ery-apoB) was measured by flowcytometry in subjects with (CAD+) and without coronary artery disease (CAD−), based on coronary angiography or on a history of cardiovascular disease. Intima media thickness (…

medicine.medical_specialtyEndotheliumApolipoprotein Bbiologybusiness.industryClinical BiochemistryGeneral MedicineNegative associationmedicine.diseaseLower riskBiochemistryCoronary artery diseasemedicine.anatomical_structureEndocrinologyIntima-media thicknessSubclinical atherosclerosisLipoprotein transportInternal medicinemedicinebiology.proteinlipids (amino acids peptides and proteins)businessEuropean Journal of Clinical Investigation
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Weaning induces NOS-2 expression through NF-κB modulation in the lactating mammary gland: importance of GSH

2005

Zaragozá, R; Miralles, VJ; Rus, AD; García, C; Carmena, R; García-Trevijano, ER; Barber, T; Pallardó, FV; Torres, L; Viña, JR. At the end of lactation the mammary gland undergoes involution, a process characterized by apoptosis of secretory cells and tissue remodelling. To gain insight into this process, we analysed the gene expression profile by oligonucleotide microarrays during lactation and after forced weaning. Up-regulation of inflammatory mediators and acute-phase response genes during weaning was found. Expression of IκBα (inhibitory κBα), a protein known to modulate NF-κB (nuclear factor-κB) nuclear translocation, was significantly up-regulated. On the other hand, there was a time-…

medicine.medical_specialtyMammary glandDown-RegulationNitric Oxide Synthase Type IIWeaninglactationBiologyBiochemistryNF-κBMammary Glands AnimalWestern blotnitric oxideInternal medicineLactationGene expressionmedicineGSHinvolutionWeaningAnimalsInvolution (medicine)Rats WistarPromoter Regions GeneticMolecular Biologymedicine.diagnostic_test:CIENCIAS DE LA VIDA::Bioquímica [UNESCO]Gene Expression ProfilingNF-kappa BUNESCO::CIENCIAS DE LA VIDA::BioquímicaCell BiologyGlutathioneRatsUp-RegulationIκBαProtein Transportmedicine.anatomical_structureEndocrinologyEnzyme InductionFemaleChromatin immunoprecipitationProtein BindingResearch Article
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Can you blame cold feet on Epac (and Rap1A)? Focus on “Cyclic AMP-Rap1A signaling activates RhoA to induce α2C-adrenoceptor translocation to the cell…

2012

Intracellular signaling by the second messenger cyclic AMP (cAMP) activates the Ras-related small GTPase Rap1 through the guanine exchange factor Epac. This activation leads to effector protein interactions, activation, and biological responses in the vasculature, including vasorelaxation. In vascular smooth muscle cells derived from human dermal arterioles (microVSM), Rap1 selectively regulates expression of G protein-coupled α2C-adrenoceptors (α2C-ARs) through JNK-c-jun nuclear signaling. The α2C-ARs are generally retained in the trans-Golgi compartment and mobilize to the cell surface and elicit vasoconstriction in response to cellular stress. The present study used human microVSM to exa…

medicine.medical_specialtyRHOAPhysiologyMyocytes Smooth MuscleCellChromosomal translocationSmooth muscleReceptors Adrenergic alpha-2Internal medicineCyclic AMPmedicineAnimalsHumansReceptorbiologyrap1 GTP-Binding ProteinsArticlesCell Biologyα2c adrenoceptorCell biologyProtein Transportmedicine.anatomical_structureEndocrinologybiology.proteinmedicine.symptomrhoA GTP-Binding ProteinVasoconstrictionAmerican Journal of Physiology-Cell Physiology
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Impact of VP1-Specific Protein Sequence Motifs on Adeno-Associated Virus Type 2 Intracellular Trafficking and Nuclear Entry

2012

ABSTRACT Adeno-associated virus type 2 (AAV2) has gained much interest as a gene delivery vector. A hallmark of AAV2-mediated gene transfer is an intracellular conformational change of the virus capsid, leading to the exposure of infection-relevant protein domains. These protein domains, which are located on the N-terminal portion of the structural proteins VP1 and VP2, include a catalytic phospholipase A 2 domain and three clusters of basic amino acids. We have identified additional protein sequence motifs located on the VP1/2 N terminus that also proved to be obligatory for virus infectivity. These motifs include signals that are known to be involved in protein interaction, endosomal sort…

virusesImmunologyProtein domainAmino Acid MotifsMolecular Sequence DataSequence alignmentBiologyMicrobiologyVirusCell LineParvoviridae InfectionsVirologyHumansAmino Acid SequenceAdeno-Associated Virus Type 2Peptide sequenceCell NucleusDependovirusMolecular biologyTransport proteinCell biologyVirus-Cell InteractionsProtein TransportCapsidInsect ScienceCapsid ProteinsSequence motifSequence Alignment
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