Detail of Fig4B_DNAPTP6



Project
Title
Time-lapse FRAP images of droplets formed by DNAPTP6
Description
Time-lapse FRAP images of droplets formed by DNAPTP6
Release, Updated
2023-07-20
License
CC BY
Kind
Image data
File Formats
.czi
Data size
518.5 MB

Organism
-
Strain(s)
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Cell Line
-

Datatype
-
Molecular Function (MF)
Biological Process (BP)
Cellular Component (CC)
Biological Imaging Method
time lapse microscopy ( Fbbi:00000249 )
FRAP ( Fbbi:00000366 )
X scale
0.0097173 micrometer/pixel
Y scale
0.0097173 micrometer/pixel
Z scale
-
T scale
5 seconds of time interval

Image Acquisition
Experiment type
-
Microscope type
-
Acquisition mode
-
Contrast method
-
Microscope model
-
Detector model
-
Objective model
-
Filter set
-

Summary of Methods
See details in Asamitsu S, et. al. Sci Adv. 2023 Feb 24;9(8):eade2035.
Related paper(s)

Sefan Asamitsu, Yasushi Yabuki, Kazuya Matsuo, Moe Kawasaki, Yuki Hirose, Gengo Kashiwazaki, Anandhakumar Chandran, Toshikazu Bando, Dan Ohtan Wang, Hiroshi Sugiyama, Norifumi Shioda (2023) RNA G-quadruplex organizes stress granule assembly through DNAPTP6 in neurons., Science advances, Volume 9, Number 8, pp. eade2035

Published in 2023 Feb 24 (Electronic publication in Feb. 24, 2023, midnight )

(Abstract) Consecutive guanine RNA sequences can adopt quadruple-stranded structures, termed RNA G-quadruplexes (rG4s). Although rG4-forming sequences are abundant in transcriptomes, the physiological roles of rG4s in the central nervous system remain poorly understood. In the present study, proteomics analysis of the mouse forebrain identified DNAPTP6 as an RNA binding protein with high affinity and selectivity for rG4s. We found that DNAPTP6 coordinates the assembly of stress granules (SGs), cellular phase-separated compartments, in an rG4-dependent manner. In neurons, the knockdown of DNAPTP6 diminishes the SG formation under oxidative stress, leading to synaptic dysfunction and neuronal cell death. rG4s recruit their mRNAs into SGs through DNAPTP6, promoting RNA self-assembly and DNAPTP6 phase separation. Together, we propose that the rG4-dependent phase separation of DNAPTP6 plays a critical role in neuronal function through SG assembly.
(MeSH Terms)

Contact
Norifumi Shioda, Sefan Asamitsu , Kumamoto University, RIKEN , Institute of Molecular Embryology and Ge- netics (IMEG), Center for Biosystems Dynamics Research (BDR) , Department of Genomic Neurology
Contributors

OMERO Dataset
OMERO Project
Source