Please use this identifier to cite or link to this item: 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

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
10_1038_ncomms9381.pdf2.68 MBAdobe PDF

OPEN

NoneView/Download

SCOPUSTM   
Citations

24
checked on Dec 3, 2022

Page view(s)

176
checked on Dec 1, 2022

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.