Structural highlights
FunctionPublication Abstract from PubMedDuring 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 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). The structural basis of Miranda-mediated Staufen localization during Drosophila neuroblast asymmetric division.,Jia M, Shan Z, Yang Y, Liu C, Li J, Luo ZG, Zhang M, Cai Y, Wen W, Wang W Nat Commun. 2015 Oct 1;6:8381. doi: 10.1038/ncomms9381. PMID:26423004[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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