Search results for "Radixin"

showing 3 items of 3 documents

Precise Somatotopic Thalamocortical Axon Guidance Depends on LPA-Mediated PRG-2/Radixin Signaling

2016

Summary Precise connection of thalamic barreloids with their corresponding cortical barrels is critical for processing of vibrissal sensory information. Here, we show that PRG-2, a phospholipid-interacting molecule, is important for thalamocortical axon guidance. Developing thalamocortical fibers both in PRG-2 full knockout (KO) and in thalamus-specific KO mice prematurely entered the cortical plate, eventually innervating non-corresponding barrels. This misrouting relied on lost axonal sensitivity toward lysophosphatidic acid (LPA), which failed to repel PRG-2-deficient thalamocortical fibers. PRG-2 electroporation in the PRG-2−/− thalamus restored the aberrant cortical innervation. We ide…

0301 basic medicineNeuroscience(all)ThalamusGrowth ConesSensory systemBiologyArticle03 medical and health scienceschemistry.chemical_compoundMice0302 clinical medicineDiscrimination PsychologicalThalamusRadixinLysophosphatidic acidNeural PathwaysmedicineAnimalsPhosphorylationGrowth coneCerebral CortexMice KnockoutGeneral NeuroscienceMembrane ProteinsAxon GuidanceCytoskeletal Proteins030104 developmental biologymedicine.anatomical_structurechemistryCerebral cortexAxon guidanceSignal transductionLysophospholipidsNeuroscience030217 neurology & neurosurgerySignal TransductionNeuron
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Deficient p27 Phosphorylation at Serine 10 Increases Macrophage Foam Cell Formation and Aggravates Atherosclerosis Through a Proliferation-Independen…

2011

OBJECTIVE: Genetic ablation of the growth suppressor p27(Kip1) (p27) in the mouse aggravates atherosclerosis coinciding with enhanced arterial cell proliferation. However, it is unknown whether molecular mechanisms that limit p27's protective function contribute to atherosclerosis development and whether p27 exerts proliferation-independent activities in the arterial wall. This study aims to provide insight into both questions by investigating the role in atherosclerosis of p27 phosphorylation at serine 10 (p27-phospho-Ser10), a major posttranslational modification of this protein. METHODS AND RESULTS: Immunoblotting studies revealed a marked reduction in p27-phospho-Ser10 in atheroscleroti…

Malerho GTP-Binding ProteinsRHOAMoesinMiceApolipoproteins ERadixinSerinemedicineAnimalsHumansProtein phosphorylationPhosphorylationProtein kinase ACell ProliferationFoam cellMice Knockoutrho-Associated KinasesbiologyArteriesAtherosclerosismedicine.diseaseCell biologyMice Inbred C57BLDisease Models AnimalAtheromaCase-Control StudiesImmunologyDisease Progressionbiology.proteinPhosphorylationFemalerhoA GTP-Binding ProteinCardiology and Cardiovascular MedicineCyclin-Dependent Kinase Inhibitor p27Foam CellsSignal TransductionArteriosclerosis, Thrombosis, and Vascular Biology
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Identification and relevance of the CD95-binding domain in the N-terminal region of ezrin.

2003

The CD95 (Fas/APO-1) linkage to the actin cytoskeleton through ezrin is an essential requirement for susceptibility to the CD95-mediated apoptosis in CD4+ T cells. We have previously shown that moesin was not involved in the binding to CD95. Here we further support the specificity of the ezrin/CD95 binding, showing that radixin did not bind CD95. The ezrin region specifically and directly involved in the binding to CD95 was located in the middle lobe of the ezrin FERM domain, between amino acids 149 and 168. In this region, ezrin, radixin, and moesin show 60-65% identity, as compared with the 86% identity in the whole FERM domain. Transfection of two different human cell lines with a green …

Moesinchemical and pharmacologic phenomenaApoptosismacromolecular substancesBiologyBiochemistryEzrinRadixinhemic and lymphatic diseasesHumansfas ReceptorMolecular BiologyActinBinding SitesFERM domainhemic and immune systemsCell BiologyTransfectionActin cytoskeletonPhosphoproteinsActinsCell biologyProtein Structure TertiaryCytoskeletal ProteinsMutationbiological phenomena cell phenomena and immunityBinding domainHeLa CellsProtein BindingSignal TransductionThe Journal of biological chemistry
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