The structural basis of Miranda-mediated Staufen localization during Drosophila neuroblast asymmetric division

Min Jia, Zelin Shan, Ying Yang, Chunhua Liu, Jianchao Li, Zhen-Ge Luo, Mingjie Zhang, Yu Cai (), Wenyu Wen () and Wenning Wang ()
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Min Jia: Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials, Ministry of Education, Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University
Zelin Shan: Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials, Ministry of Education, Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University
Ying Yang: Temasek Life Sciences Laboratory, National University of Singapore
Chunhua Liu: Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials, Ministry of Education, Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University
Jianchao Li: State Key Laboratory of Molecular Neuroscience, Hong Kong University of Science and Technology, Clear Water Bay
Zhen-Ge Luo: Institute of Neuroscience and State Key Laboratory of Neuroscience, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences
Mingjie Zhang: State Key Laboratory of Molecular Neuroscience, Hong Kong University of Science and Technology, Clear Water Bay
Yu Cai: Temasek Life Sciences Laboratory, National University of Singapore
Wenyu Wen: Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials, Ministry of Education, Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University
Wenning Wang: Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials, Ministry of Education, Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: 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 β-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).

Date: 2015
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DOI: 10.1038/ncomms9381

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