期刊
NATURE COMMUNICATIONS
卷 6, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms9381
关键词
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资金
- National Major Basic Research Program of China [2011CB808505, 2014CB910201]
- National Science Foundation of China [21473034, 31270778, 31422015]
- Program for New Century Excellent Talents in University [NCET-12-0129]
- Shanghai 'Shu Guang' Project [14SG06]
- Specialized Research Fund for the Doctoral Program of Higher Education [20130071140004]
- Science & Technology Commission of Shanghai Municipality [08DZ2270500]
- Temasek Life Sciences Laboratory
- Singapore Millennium Foundation
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 doublestranded 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 beta-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).
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