Search results for "Motor protein"

showing 10 items of 14 documents

Age affects myosin relaxation states in skeletal muscle fibers of female but not male mice

2018

The recent discovery that myosin has two distinct states in relaxed muscle–disordered relaxed (DRX) and super-relaxed (SRX)–provides another factor to consider in our fundamental understanding of the aging mechanism in skeletal muscle, since myosin is thought to be a potential contributor to dynapenia (age-associated loss of muscle strength independent of atrophy). The primary goal of this study was to determine the effects of age on DRX and SRX states and to examine their sex specificity. We have used quantitative fluorescence microscopy of the fluorescent nucleotide analog 2′/3′-O-(N-methylanthraniloyl) ATP (mantATP) to measure single-nucleotide turnover kinetics of myosin in skinned skel…

Adenosine TriphosphataseMale0301 basic medicineAgingMuscle PhysiologyPhysiologyMuscle RelaxationATPaseMuscle Fibers Skeletallcsh:MedicineMale miceSkeletal Muscle FibersBiochemistrymyosinsMiceMyosin headContractile Proteins0302 clinical medicineAnimal Cellsskeletal muscle fibresMyosinMedicine and Health SciencesgenderLipid HormonesPost-Translational ModificationPhosphorylationlcsh:Scienceta315Musculoskeletal SystemSex Characteristics0303 health sciencesMultidisciplinaryEstradiolRelaxation (psychology)biologyChemistryMusclesanimal experimentsEnzymesmedicine.anatomical_structurePhosphorylationFemaleCellular TypesAnatomyResearch ArticleMuscle ContractionSex characteristicsmedicine.medical_specialtyMotor ProteinssukupuolierotActin MotorseläinkokeetMuscle Fibersmyosiinitsukupuoli03 medical and health sciencesAtrophyMolecular MotorsInternal medicinemedicineAnimalslihassolut030304 developmental biology030102 biochemistry & molecular biologylcsh:RPhosphatasesBiology and Life SciencesProteinsSkeletal muscleCell BiologySkeletal Muscle Fibersmedicine.diseaseHormonesCytoskeletal Proteins030104 developmental biologyEndocrinologySkeletal MusclesageEnzymologybiology.proteinlcsh:QSteady state (chemistry)ikä030217 neurology & neurosurgery
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Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1.

1999

AbstractThe interaction of cytoplasmic dynein with its cargoes is thought to be indirectly mediated by dynactin, a complex that binds to the dynein intermediate chain. However, the roles of other dynein subunits in cargo binding have been unknown. Here we demonstrate that dynein translocates rhodopsin-bearing vesicles along microtubules. This interaction occurs directly between the C-terminal cytoplasmic tail of rhodopsin and Tctex-1, a dynein light chain. C-terminal rhodopsin mutations responsible for retinitis pigmentosa inhibit this interaction. Our results point to an alternative docking mechanism for cytoplasmic dynein, provide novel insights into the role of motor proteins in the pola…

CytoplasmRhodopsingenetic structuresMicrotubule-associated proteinRecombinant Fusion ProteinsDyneinMolecular Sequence DataReceptors Cell Surfacemacromolecular substancesBiologyT-Complex Genome RegionMicrotubulesGeneral Biochemistry Genetics and Molecular BiologyMotor protein03 medical and health sciencesMice0302 clinical medicineMicrotubuleAnimalsAmino Acid Sequence030304 developmental biologyt-Complex Genome Region0303 health sciencesBinding SitesBiochemistry Genetics and Molecular Biology(all)DyneinsNuclear ProteinsBiological Transport3. Good healthCell biologyCytoplasmRhodopsinMutagenesisDynactinbiology.proteinMicrotubule ProteinsCattlesense organsMicrotubule-Associated Proteins030217 neurology & neurosurgeryPhotoreceptor Cells VertebrateCell
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Identification of the dynein light chains required for human papillomavirus infection

2010

Summary Human papillomaviruses (HPVs) are a family of small non-enveloped DNA viruses. Some genital HPV types, including HPV type 16 (HPV16), are the causative agent for the development of cancer at the site of infection. HPVs encode two capsid proteins, L1 and L2. After endocytic cell entry and egress from endosomes, L2 accompanies the viral DNA to the nucleus where replication is initiated. For cytoplasmic transport, L2 interacts with the microtubule network via the motor protein complex dynein. We have performed yeast two-hybrid screening and identified the dynein light chain DYNLT1 (previously called Tctex1) as interaction partner of HPV16 L2. Using co-immunoprecipitation and immunofluo…

EndosomevirusesImmunologyDyneinEndocytic cyclevirus diseasesBiologyImmunoglobulin light chainMicrobiologyMolecular biologyCell biologyMotor proteinchemistry.chemical_compoundchemistryMicrotubuleVirologyDYNLT3DNACellular Microbiology
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Identification of a Dynein Interacting Domain in the Papillomavirus Minor Capsid Protein L2

2006

ABSTRACT Papillomaviruses enter cells via endocytosis (H. C. Selinka et al., Virology 299:279-287, 2002). After egress from endosomes, the minor capsid protein L2 accompanies the viral DNA to the nucleus and subsequently to the subnuclear promyelocytic leukemia protein bodies (P. M. Day et al., Proc. Natl. Acad. Sci. USA 101:14252-14257, 2004), suggesting that this protein may be involved in the intracytoplasmic transport of the viral genome. We now demonstrate that the L2 protein is able to interact with the microtubule network via the motor protein dynein. L2 protein was found attached to microtubules after uncoating of incoming human papillomavirus pseudovirions. Based on immunofluoresce…

ImmunoprecipitationImmunologyDyneinActive Transport Cell NucleusGenome ViralMicrotubulesMicrobiologyMotor proteinPromyelocytic leukemia proteinMicrotubuleDynein ATPaseVirologyHumansPapillomaviridaebiologyPapillomavirus InfectionsDyneinsOncogene Proteins ViralMolecular biologyEndocytosisVirus-Cell InteractionsMicroscopy FluorescenceCapsidInsect ScienceDNA Viralbiology.proteinDynactinCapsid ProteinsIntranuclear SpaceHeLa CellsProtein BindingJournal of Virology
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Autonomous artificial nanomotor powered by sunlight

2006

Light excitation powers the reversible shuttling movement of the ring component of a rotaxane between two stations located at a 1.3-nm distance on its dumbbell-shaped component. The photoinduced shuttling movement, which occurs in solution, is based on a “four-stroke” synchronized sequence of electronic and nuclear processes. At room temperature the deactivation time of the high-energy charge-transfer state obtained by light excitation is ≈10 μs, and the time period required for the ring-displacement process is on the order of 100 μs. The rotaxane behaves as an autonomous linear motor and operates with a quantum efficiency up to ≈12%. The investigated system is a unique example of an artif…

Models MolecularLuminescenceMagnetic Resonance SpectroscopyTime FactorsRotaxaneLightRotaxanesUltraviolet RaysPhotochemistryMovementMolecular ConformationElectronsPhotochemistryAbsorptionQUIMICA ORGANICAPhenothiazinesRotaxaneElectrochemistryNanotechnologyNanomotorAbsorption (electromagnetic radiation)Molecular machinePhotolysisMultidisciplinaryChemistrybusiness.industryMolecular Motor ProteinsPhotodissociationTemperatureLinear motorKineticsNanoscienceFluid solutionSpectrophotometryPhysical SciencesSunlightOptoelectronicsQuantum efficiencyElectronicsLuminescencebusinessSupramolecular chemistry
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MyRIP, a novel Rab effector, enables myosin VIIa recruitment to retinal melanosomes

2002

Defects of the myosin VIIa motor protein cause deafness and retinal anomalies in humans and mice. We report on the identification of a novel myosin-VIIa-interacting protein that we have named MyRIP (myosin-VIIa- and Rab-interacting protein), since it also binds to Rab27A in a GTP-dependent manner. In the retinal pigment epithelium cells, MyRIP, myosin VIIa and Rab27A are associated with melanosomes. In transfected PC12 cells, overexpression of MyRIP was shown to interfere with the myosin VIIa tail localization. We propose that a molecular complex composed of Rab27A, MyRIP and myosin VIIa bridges retinal melanosomes to the actin cytoskeleton and thereby mediates the local trafficking of thes…

Molecular Sequence Datamacromolecular substancesMyosinsBiologyBiochemistryRetinarab27 GTP-Binding ProteinsMotor proteinMicechemistry.chemical_compoundTwo-Hybrid System Techniquesotorhinolaryngologic diseasesGeneticsmedicineAnimalsHumansAmino Acid SequenceRAB27Molecular BiologyGene LibraryMelanosomesRetinal pigment epitheliumScientific ReportsDyneinsRetinalActin cytoskeletonCell biologymedicine.anatomical_structurechemistryOrgan Specificityrab GTP-Binding ProteinsMelanosome transportMyosin VIIaMelanophilinsense organsRabSequence Alignmentcirculatory and respiratory physiologyEMBO reports
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The giant spectrin βV couples the molecular motors to phototransduction and Usher syndrome type I proteins along their trafficking route.

2013

International audience; Mutations in the myosin VIIa gene cause Usher syndrome type IB (USH1B), characterized by deaf-blindness. A delay of opsin trafficking has been observed in the retinal photoreceptor cells of myosin VIIa-deficient mice. We identified spectrin bV, the mammalian b-heavy spectrin, as a myosin VIIa-and rhodopsin-interacting partner in photoreceptor cells. Spectrin bV displays a polarized distribution from the Golgi apparatus to the base of the outer segment, which, unlike that of other b spectrins, matches the trafficking route of opsin and other phototransduction proteins. Formation of spectrin bV-rhodopsin complex could be detected in the differentiating photoreceptors a…

OpsinRhodopsinLight Signal Transductiongenetic structures[SDV]Life Sciences [q-bio]Cell Cycle Proteinsmacromolecular substancesBiologyMyosinsOpsin transportRetinaMotor protein03 medical and health sciencesMice0302 clinical medicineMyosinotorhinolaryngologic diseasesGeneticsAnimalsHumansSpectrinMolecular BiologyGenetics (clinical)030304 developmental biologyAdaptor Proteins Signal Transducing0303 health sciencesEPB41SpectrinGeneral Medicineeye diseasesCell biologyCytoskeletal ProteinsRhodopsinMyosin VIIabiology.proteinMicrotubule Proteinssense organsUsher Syndromes030217 neurology & neurosurgeryVisual phototransductionHeLa CellsPhotoreceptor Cells VertebrateHuman molecular genetics
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Exploitation of Microtubule Cytoskeleton and Dynein during Parvoviral Traffic toward the Nucleus

2003

ABSTRACT Canine parvovirus (CPV), a model virus for the study of parvoviral entry, enters host cells by receptor-mediated endocytosis, escapes from endosomal vesicles to the cytosol, and then replicates in the nucleus. We examined the role of the microtubule (MT)-mediated cytoplasmic trafficking of viral particles toward the nucleus. Immunofluorescence and immunoelectron microscopy showed that capsids were transported through the cytoplasm into the nucleus after cytoplasmic microinjection but that in the presence of MT-depolymerizing agents, viral capsids were unable to reach the nucleus. The nuclear accumulation of capsids was also reduced by microinjection of an anti-dynein antibody. More…

Parvovirus CaninevirusesImmunoelectron microscopyImmunologyDyneinActive Transport Cell Nucleusmacromolecular substancesMicrotubulesMicrobiologyMotor proteinCapsidCytosolMicrotubuleVirologymedicineAnimalsCytoskeletonCytoskeletonCell NucleusbiologyDyneinsbiochemical phenomena metabolism and nutritionVirus-Cell InteractionsCell biologyMicroscopy ElectronTubulinmedicine.anatomical_structureCytoplasmInsect ScienceCatsbiology.proteinNucleusJournal of Virology
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The GRIP1/14-3-3 Pathway Coordinates Cargo Trafficking and Dendrite Development

2014

SummaryRegulation of cargo transport via adaptor molecules is essential for neuronal development. However, the role of PDZ scaffolding proteins as adaptors in neuronal cargo trafficking is still poorly understood. Here, we show by genetic deletion in mice that the multi-PDZ domain scaffolding protein glutamate receptor interacting protein 1 (GRIP1) is required for dendrite development. We identify an interaction between GRIP1 and 14-3-3 proteins that is essential for the function of GRIP1 as an adaptor protein in dendritic cargo transport. Mechanistically, 14-3-3 binds to the kinesin-1 binding region in GRIP1 in a phospho-dependent manner and detaches GRIP1 from the kinesin-1 motor protein …

Scaffold proteinPDZ domainKinesinsNerve Tissue ProteinsDendriteBiologyGeneral Biochemistry Genetics and Molecular BiologyMotor proteinGene Knockout TechniquesMiceMicrotubulemedicineAnimalsMolecular BiologyAdaptor Proteins Signal TransducingPoint mutationSignal transducing adaptor proteinDendritesCell BiologyCell biologyProtein Transportmedicine.anatomical_structure14-3-3 ProteinsMutationCarrier ProteinsFunction (biology)Protein BindingSignal TransductionTranscription FactorsDevelopmental BiologyDevelopmental Cell
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Stepping molecular motor amid Lévy white noise

2015

We consider a model of a stepping molecular motor consisting of two connected heads. Directional motion of the stepper takes place along a one-dimensional track. Each head is subject to a periodic potential without spatial reflection symmetry. When the potential for one head is switched on, it is switched off for the other head. Additionally, the system is subject to the influence of symmetric, white Lévy noise that mimics the action of external random forcing. The stepper exhibits motion with a preferred direction which is examined by analyzing the median of the displacement of a midpoint between the positions of the two heads. We study the modified dynamics of the stepper by numerical sim…

Statistics and ProbabilityModels MolecularPhysicsMolecular Motor ProteinsMathematical analysisCondensed Matter PhysicWhite noiseMidpointDisplacement (vector)MotionNoiseReflection symmetryMolecular motorHead (vessel)Computer SimulationStatistical physicsStepperStatistical and Nonlinear Physic
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