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dc.contributor.advisorGeli, María Isabel-
dc.contributor.authorMera Namin, Rosalia-
dc.description.abstractMyo5, a member of the non-conventional type I myosins (Myosins I), is a molecular motor that plays an essential role in the uptake step of receptor-mediated endocytosis in yeast. Besides working as a motor that translocate actin filaments, Myo5 initiates Arp2/3-dependent of actin polymerization at sites of endocytosis. Development of the Myo5 activity as an actin nucleating promotor factor requires the interaction of Myo5 with Vrp1, the yeast homologue of WIP, which provides binding sites for monomeric actin. How and when actin polymerization is ignited is essential to generate productive forces capable of deforming the plasma membrane and therefore, understanding how the recruitment and the activity of the myosins-I is regulated is of key importance to comprehend the budding process. Recent data indicates that binding of calmodulin to Myo5 stabilizes an autoinhibitory conformation that prevents binding to its coactivator Vrp1, and as a consequence, Myo5-induced actin polymerization. Calmodulin binds to two IQ motives situated at the neck that separates the motor head from the tail containing a lipid-binding autoinhibitory domain TH1 and the C-terminal extension, involved in the activation of actin polymerization. The aim of this study is to take a deeper view at the molecular details of the interaction between Myo5 and Cmd1, to better understand how the IQ motifs and calmodulin contribute to stabilize the autoinhibited conformation. Saccharomyces cerevisiae is a model system widely used to study endocytosis because the molecular machinery involved in the process is highly conserved from yeast to mammals. Furthermore, the manageable yeast genetics and its amenability to biochemistry, liveimaging, electron microscopy and molecular biology has contributed to position S. cerevisiae as a leading model system in the field.-
dc.publisherCSIC - Instituto de Biología Molecular de Barcelona (IBMB)-
dc.publisherUniversidad de Barcelona-
dc.titleEstudio de la interacción del cuello de Miosina 5 con Calmodulina-
dc.typeproyecto fin de carrera-
dc.description.versionPeer Reviewed-
Appears in Collections:(IBMB) Tesis
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