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https://doi.org/10.1038/ncomms9381
| Title: | The structural basis of Miranda-mediated Staufen localization during Drosophila neuroblast asymmetric division | Authors: | Jia, M Shan, Z Yang, Y Liu, C Li, J Luo, Z.-G Zhang, M Cai, Y Wen, W Wang, W |
Keywords: | double stranded RNA Miranda protein oxygen scaffold protein Staufen protein unclassified drug cell cycle protein Drosophila protein Mira protein, Drosophila RNA binding protein stau protein, Drosophila brain cancer cells and cell components crystal structure fly protein tumor alpha helix Article beta sheet brain tumor cell division cell fate cellular distribution crystal structure Drosophila ganglion isothermal titration calorimetry neuroblast nonhuman protein binding protein interaction protein localization protein structure size exclusion chromatography stoichiometry X ray crystallography animal cell line cytology Drosophila melanogaster gene expression regulation genetics metabolism molecular model nerve cell physiology protein conformation protein transport Animals Cell Cycle Proteins Cell Line Drosophila melanogaster Drosophila Proteins Gene Expression Regulation Models, Molecular Neurons Protein Conformation Protein Transport RNA-Binding Proteins |
Issue Date: | 2015 | Publisher: | Nature Publishing Group | Citation: | Jia, M, Shan, Z, Yang, Y, Liu, C, Li, J, Luo, Z.-G, Zhang, M, Cai, Y, Wen, W, Wang, W (2015). The structural basis of Miranda-mediated Staufen localization during Drosophila neuroblast asymmetric division. Nature Communications 6 : 8381. ScholarBank@NUS Repository. https://doi.org/10.1038/ncomms9381 | Abstract: | During the asymmetric division of Drosophila neuroblasts (NBs), the scaffold Miranda (Mira) coordinates the subcellular distribution of cell-fate determinants including Staufen (Stau) and segregates them into the ganglion mother cells (GMCs). Here we show the fifth double-stranded RNA (dsRNA)-binding domain (dsRBD5) of Stau is necessary and sufficient for binding to a coiled-coil region of Mira cargo-binding domain (CBD). The crystal structure of Mira514-595/Stau dsRBD5 complex illustrates that Mira forms an elongated parallel coiled-coil dimer, and two dsRBD5 symmetrically bind to the Mira dimer through their exposed ?-sheet faces, revealing a previously unrecognized protein interaction mode for dsRBDs. We further demonstrate that the Mira-Stau dsRBD5 interaction is responsible for the asymmetric localization of Stau during Drosophila NB asymmetric divisions. Finally, we find the CBD-mediated dimer assembly is likely a common requirement for Mira to recognize and translocate other cargos including brain tumour (Brat). © 2015 Macmillan Publishers Limited. All rights reserved. | Source Title: | Nature Communications | URI: | https://scholarbank.nus.edu.sg/handle/10635/175480 | ISSN: | 20411723 | DOI: | 10.1038/ncomms9381 |
| Appears in Collections: | Staff Publications Elements |
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