Search results for "Septins"

showing 4 items of 4 documents

Quantitative and integrative proteome analysis of peripheral nerve myelin identifies novel myelin proteins and candidate neuropathy loci

2011

Peripheral nerve myelin facilitates rapid impulse conduction and normal motor and sensory functions. Many aspects of myelin biogenesis, glia–axonal interactions, and nerve homeostasis are poorly understood at the molecular level. We therefore hypothesized that only a fraction of all relevant myelin proteins has been identified so far. Combining gel-based and gel-free proteomic approaches, we identified 545 proteins in purified mouse sciatic nerve myelin, including 36 previously known myelin constituents. By mass spectrometric quantification, the predominant P0, periaxin, and myelin basic protein constitute 21, 16, and 8% of the total myelin protein, respectively, suggesting that their relat…

MaleProteomicsCandidate geneProteomePrions10208 Institute of Neuropathology610 Medicine & healthHereditary neuralgic amyotrophyTetraspanin 24BiologySeptinTranscriptomeMice03 medical and health sciencesMyelin0302 clinical medicinemedicineAnimalsElectrophoresis Gel Two-DimensionalRNA MessengerMyelin Sheath030304 developmental biologyMice KnockoutGenetics0303 health sciencesGeneral NeuroscienceComputational BiologyMembrane Proteins2800 General NeuroscienceArticlesmedicine.diseaseSciatic NerveCell biologyMyelin basic proteinMice Inbred C57BLMolecular Weightmedicine.anatomical_structureAnimals Newbornnervous systemSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationProteomebiology.protein570 Life sciences; biologyChemokinesMyelin ProteinsSeptins030217 neurology & neurosurgeryBiogenesisDemyelinating Diseases
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Septins 2, 7 and 9 and MAP4 colocalize along the axoneme in the primary cilium and control ciliary length

2013

International audience; Septins are a large, evolutionarily conserved family of GTPases that form hetero-oligomers and interact with the actin-based cytoskeleton and microtubules. They are involved in scaffolding functions, and form diffusion barriers in budding yeast, the sperm flagellum and the base of primary cilia of kidney epithelial cells. We investigated the role of septins in the primary cilium of retinal pigmented epithelial (RPE) cells, and found that SEPT2 forms a 1:1:1 complex with SEPT7 and SEPT9 and that the three members of this complex colocalize along the length of the axoneme. Similar to observations in kidney epithelial cells, depletion of cilium-localized septins by siRN…

AxonemeAxonemeMicrotubule-associated protein[SDV]Life Sciences [q-bio]DIFFUSION BARRIERTUBULINCell Cycle Proteinsmacromolecular substancesORGANIZATIONCYTOSKELETONBiologySeptinMicrotubulesRetinaCell Line03 medical and health sciences0302 clinical medicineMicrotubuleCiliogenesisHumansCiliaCytoskeletonMolecular BiologyAFFINITY-REGULATING KINASEActin030304 developmental biologyCILIOGENESIS0303 health sciencesPrimary ciliumCOMPLEXSperm flagellumCilium030302 biochemistry & molecular biologyColocalizationEpithelial CellsAnatomyCell BiologyActinsCell biology[SDV] Life Sciences [q-bio]MAMMALIAN SEPTINSMAP4CELLSbiological phenomena cell phenomena and immunityMicrotubule-Associated Proteins030217 neurology & neurosurgerySeptinsDevelopmental BiologyResearch Article
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Septin/anillin filaments scaffold central nervous system myelin to accelerate nerve conduction

2016

Myelination of axons facilitates rapid impulse propagation in the nervous system. The axon/myelin-unit becomes impaired in myelin-related disorders and upon normal aging. However, the molecular cause of many pathological features, including the frequently observed myelin outfoldings, remained unknown. Using label-free quantitative proteomics, we find that the presence of myelin outfoldings correlates with a loss of cytoskeletal septins in myelin. Regulated by phosphatidylinositol-(4,5)-bisphosphate (PI(4,5)P2)-levels, myelin septins (SEPT2/SEPT4/SEPT7/SEPT8) and the PI(4,5)P2-adaptor anillin form previously unrecognized filaments that extend longitudinally along myelinated axons. By confoca…

0301 basic medicineNervous systemCentral Nervous SystemProteomicsScaffoldMouseProteomeNeural ConductionSeptinNerve Fibers MyelinatedMyelinGene Knockout TechniquesMiceContractile ProteinsAxonBiology (General)CytoskeletonMicroscopy ImmunoelectronCytoskeletonMyelin SheathMicroscopy ConfocalGeneral NeuroscienceQRGeneral MedicineAnatomyCell biologyglial cellsmedicine.anatomical_structureGene TargetingMedicineResearch ArticleQH301-705.5ScienceCentral nervous systemmyelinated axonsmacromolecular substancesBiologyGeneral Biochemistry Genetics and Molecular Biologymyelin structure03 medical and health sciencesSeptin/anillin filaments; central nervous system; myelinlabel-free proteomicsmedicineAnimalsneuropathologyGeneral Immunology and Microbiology030104 developmental biologynervous systemseptin cytoskeletonProtein MultimerizationSeptinsSeptin cytoskeletonNeuroscienceeLife
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Impaired Platelet Function in Sept8-Deficient Mice In Vitro.

2020

AbstractSeptins (Septs) are a widely expressed protein family of 13 mammalian members, recognized as a unique component of the cytoskeleton. In human platelets, we previously described that SEPT4 and SEPT8 are localized surrounding α-granules and move to the platelet surface after activation, indicating a possible role in platelet physiology. In this study, we investigated the impact of Sept8 on platelet function in vitro using Sept8-deficient mouse platelets. Deletion of Sept8 in mouse platelets caused a pronounced defect in activation of the fibrinogen receptor integrin αIIbβ3, α-granule exocytosis, and aggregation, especially in response to the glycoprotein VI agonist convulxin. In contr…

0301 basic medicineBlood PlateletsGenotypePlatelet AggregationFibrinogen receptorIntegrinPlatelet Glycoprotein GPIIb-IIIa Complex030204 cardiovascular system & hematologyFibrinogenCytoplasmic GranulesExocytosisExocytosis03 medical and health sciences0302 clinical medicineLysosomeCrotalid VenomsmedicineAnimalsPlateletLectins C-TypeLactadherinMice KnockoutbiologyChemistryThrombinFibrinogenConvulxinHematologyPlatelet ActivationCell biologyMice Inbred C57BL030104 developmental biologymedicine.anatomical_structurePhenotypebiology.proteinFemaleLysosomesSeptinsmedicine.drugThrombosis and haemostasis
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