Search results for " F-actin"

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Identification and characterization of PlAlix, the Alix homologue from the Mediterranean sea urchin Paracentrotus lividus.

2013

The sea urchin provides a relatively simple and tractable system for analyzing the early stages of embryo development. Here, we use the sea urchin species, Paracentrotus lividus, to investigate the role of Alix in key stages of embryogenesis, namely the egg fertilization and the first cleavage division. Alix is a multifunctional protein involved in different cellular processes including endocytic membrane trafficking, filamentous (F)-actin remodeling, and cytokinesis. Alix homologues have been identified in different metazoans; in these organisms, Alix is involved in oogenesis and in determination/differentiation events during embryo development. Herein, we describe the identification of th…

MaleBlastomeresanimal structuresDNA ComplementaryEmbryo Nonmammalian2-cell stage embryo; Alix/AIP1; F-actin; sea urchin embryoBlotting WesternMolecular Sequence DataParacentrotus lividusF-actinbiology.animalBotany2-cell stage embryoMediterranean SeaAnimalsAmino Acid SequenceCloning MolecularSea urchinPeptide sequenceActinsea urchin embryoMicroscopy ConfocalbiologySequence Homology Amino AcidReverse Transcriptase Polymerase Chain ReactionEmbryogenesisMicrofilament ProteinsGene Expression Regulation DevelopmentalEmbryoCell BiologySequence Analysis DNAbiology.organism_classificationAlix/AIP1Cell biologyCytoplasmFertilizationembryonic structuresParacentrotusFemaleCytokinesisDevelopmental Biology
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Alix protein is substrate of Ozz-E3 ligase and modulates actin remodeling in skeletal muscle

2012

Alix/AIP1 is a multifunctional adaptor protein that participates in basic cellular processes, including membrane trafficking and actin cytoskeleton assembly, by binding selectively to a variety of partner proteins. However, the mechanisms regulating Alix turnover, subcellular distribution, and function in muscle cells are unknown. We now report that Alix is expressed in skeletal muscle throughout myogenic differentiation. In myotubes, a specific pool of Alix colocalizes with Ozz, the substrate-binding component of the muscle-specific ubiquitin ligase complex Ozz-E3. We found that interaction of the two endogenous proteins in the differentiated muscle fibers changes Alix conformation and pro…

Ubiquitin-Protein LigasesMuscle Fibers Skeletalmacromolecular substancesBiochemistryCell LineMiceCell MovementTwo-Hybrid System TechniquesmedicineCell AdhesionAnimalsProtein Interaction Domains and MotifsPseudopodiaMuscle SkeletalMolecular BiologyActinMice KnockoutbiologyMyogenesisSettore BIO/16 - Anatomia UmanaCalcium-Binding ProteinsUbiquitinationActin remodelingSkeletal muscleUbiquitin-Protein Ligase ComplexesCell BiologyActin cytoskeletonUbiquitin ligaseCell biologyRepressor ProteinsActin CytoskeletonProtein Transportmedicine.anatomical_structureUbiquitin ligase complexbiology.proteinCell Migration Myogenesis Skeletal Muscle Ubiquitin Ligase Ubiquitination Alix F-actin Ozz-E3 Ubiquitin Ligase Skeletal Muscle CellsCortactinCortactinProtein Binding
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