Search results for "Qa-SNARE Proteins"

showing 5 items of 5 documents

Comprehensive analysis of expression, subcellular localization, and cognate pairing of SNARE proteins in oligodendrocytes

2009

Oligodendrocytes form the central nervous system myelin sheath by spiral wrapping of their plasma membrane around axons, necessitating a high rate of exocytic membrane addition to the growing myelin membrane. Membrane fusion is mediated by soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins (SNAREs), which act by specific pairing of vesicle (R)- and target (Q)-SNAREs. To characterize oligodendroglial SNAREs and their trafficking pathways, we performed a detailed expression analysis of SNAREs in differentiating cultured oligodendrocytes and myelin and determined their subcellular localization. Expression of the plasma membrane Q-SNAREs syntaxin 3, syntaxin 4, SNAP2…

Central Nervous SystemMaleVesicle-Associated Membrane Protein 3SynaptobrevinGolgi ApparatusBiologyMembrane FusionR-SNARE ProteinsMiceCellular and Molecular NeuroscienceSNAP23AnimalsSyntaxinQc-SNARE ProteinsTransport VesiclesCells CulturedMyelin SheathR-SNARE ProteinsQa-SNARE ProteinsVesicleCell MembraneLipid bilayer fusionQb-SNARE ProteinsSyntaxin 3Cell CompartmentationTransport proteinCell biologyOligodendrogliaProtein Transportnervous systemFemalebiological phenomena cell phenomena and immunitySNARE ProteinsDimerizationJournal of Neuroscience Research
researchProduct

Stx5 is a novel interactor of VLDL-R to affect its intracellular trafficking and processing

2012

We identified syntaxin 5 (Stx5), a protein involved in intracellular vesicle trafficking, as a novel interaction partner of the very low density lipoprotein (VLDL)-receptor (VLDL-R), a member of the LDL-receptor family. In addition, we investigated the effect of Stx5 on VLDL-R maturation, trafficking and processing. Here, we demonstrated mutual association of both proteins using several in vitro approaches. Furthermore, we detected a special maturation phenotype of VLDL-R resulting from Stx5 overexpression. We found that Stx5 prevented advanced Golgi-maturation of VLDL-R, but did not cause accumulation of the immature protein in ER, ER to Golgi compartments, or cis-Golgi ribbon, the main ex…

Low-density lipoprotein receptor-related protein 8Very Low-Density Lipoprotein ReceptorCHO CellsSTX5Biologysymbols.namesakeCricetulusCricetinaeAnimalsHumansSyntaxinSecretory PathwayQa-SNARE ProteinsCell Membranenutritional and metabolic diseasesIntracellular vesicleHep G2 CellsCell BiologyGolgi apparatusCell biologyProtein TransportHEK293 CellsReceptors LDLLDL receptorsymbolslipids (amino acids peptides and proteins)Protein Processing Post-TranslationalIntracellularProtein Bindingtrans-Golgi NetworkExperimental Cell Research
researchProduct

ROP, the Drosophila Sec1 homolog, interacts with syntaxin and regulates neurotransmitter release in a dosage-dependent manner.

1998

The Sec1 family of proteins is thought to function in both non-neuronal and neuronal secretion, although the precise role of this protein family has not been defined. Here, we study the function of ROP, the Drosophila Sec1 homolog, in neurotransmitter release. Electrophysiological analyses of transgenic lines overexpressing ROP and syntaxin, a presynaptic membrane protein, indicate that ROP interacts with syntaxin in vivo. Characterization of four point mutations in ROP shows that they fall into two phenotypic classes. Two mutations cause a dramatic reduction in both evoked and spontaneous neurotransmitter release. In contrast, the other two mutations reveal an increase in evoked neurotrans…

Munc18 Proteinscongenital hereditary and neonatal diseases and abnormalitiesProtein familyNerve Tissue ProteinsNeurotransmissionBiologySynaptic TransmissionGeneral Biochemistry Genetics and Molecular BiologySyntaxin bindingExocytosischemistry.chemical_compoundSyntaxinAnimalsDrosophila ProteinsNeurotransmitterMolecular BiologyNeurotransmitter AgentsGeneral Immunology and MicrobiologyQa-SNARE ProteinsGeneral NeuroscienceMembrane ProteinsSyntaxin 3eye diseasesCell biologychemistryDrosophilaResearch ArticleThe EMBO journal
researchProduct

Syntaxin13 expression is regulated by mammalian target of rapamycin (mTOR) in injured neurons to promote axon regeneration.

2014

Injured peripheral neurons successfully activate intrinsic signaling pathways to enable axon regeneration. We have previously shown that dorsal root ganglia (DRG) neurons activate the mammalian target of rapamycin (mTOR) pathway following injury and that this activity enhances their axon growth capacity. mTOR plays a critical role in protein synthesis, but the mTOR-dependent proteins enhancing the regenerative capacity of DRG neurons remain unknown. To identify proteins whose expression is regulated by injury in an mTOR-dependent manner, we analyzed the protein composition of DRGs from mice in which we genetically activated mTOR and from mice with or without a prior nerve injury. Quantitati…

ProteomicsAxon; Proteomics; Regeneration; SNARE Proteins; mTORSNARE Proteinmedicine.medical_treatmentInbred C57BLRegenerative MedicineBiochemistryMedical and Health SciencesMiceNeurobiologyGanglia SpinalAxonCells CulturedMice KnockoutGene knockdownCulturedQa-SNARE ProteinsTOR Serine-Threonine KinasesAxotomyBiological SciencesSciatic NerveCell biologymedicine.anatomical_structureNeurologicalmTORFemaleAxotomySignal transductionmedicine.symptomSNARE ProteinsBiochemistry & Molecular BiologyPhysical Injury - Accidents and Adverse EffectsSpinalSensory Receptor CellsCellsKnockout1.1 Normal biological development and functioningBiologyAxonUnderpinning researchmedicineAnimalsRegenerationMolecular BiologyPI3K/AKT/mTOR pathwayRegeneration (biology)NeurosciencesProteomicCell BiologyNerve injuryAxonsNerve RegenerationMice Inbred C57BLnervous systemChemical SciencesAxoplasmic transportGanglia
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