Calmodulin dissociation regulates Myo5 recruitment and function at endocytic sites.
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Myosins-I are conserved proteins that bear an N-terminal motor head followed by a Tail Homology 1 (TH1) lipid-binding domain. Some myosins-I have an additional C-terminal extension (C(ext)) that promotes Arp2/3 complex-dependent actin polymerization. The head and the tail are separated by a neck that binds calmodulin or calmodulin-related light chains. Myosins-I are known to participate in actin-dependent membrane remodelling. However, the molecular mechanisms controlling their recruitment and their biochemical activities in vivo are far from being understood. In this study, we provided evidence suggesting the existence of an inhibitory interaction between the TH1 domain of the yeast myosin-I Myo5 and its C(ext). The TH1 domain prevented binding of the Myo5 C(ext) to the yeast WIP homologue Vrp1, Myo5 C(ext)-induced actin polymerization and recruitment of the Myo5 C(ext) to endocytic sites. Our data also indicated that calmodulin dissociation from Myo5 weakened the interaction between the neck and TH1 domains and the C(ext). Concomitantly, calmodulin dissociation triggered Myo5 binding to Vrp1, extended the myosin-I lifespan at endocytic sites and activated Myo5-induced actin polymerization.
SubjectActin-Related Protein 2-3 Complex
Myosin Type I
Protein Interaction Domains and Motifs
Saccharomyces cerevisiae Proteins
Published Version (Please cite this version)10.1038/emboj.2010.159
Publication InfoCollette, JR; Fernández-Golbano, IM; Geli, MI; Giblin, JP; Grötsch, H; Idrissi, FZ; ... Robles, V (2010). Calmodulin dissociation regulates Myo5 recruitment and function at endocytic sites. EMBO J, 29(17). pp. 2899-2914. 10.1038/emboj.2010.159. Retrieved from http://hdl.handle.net/10161/12467.
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Assistant Professor of the Practice of Psychology and Neuroscience
Dr. Newpher teaches and advises for Duke's Undergraduate Studies in Neuroscience program. He also directs the Summer Neuroscience Program of Research in the Duke Institute for Brain Sciences. Dr. Newpher earned his Ph.D. in molecular biology from Case Western Reserve University. He then came to Duke to receive postdoctoral training in the Department of Neurobiology, where his research focused on identifying key molecular mechanisms that underlie learning-related synaptic
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