Summary of 294-Asamitsu-DNAPTP6Dyn

SSBD:database
SSBD:database URL
Title
Time-lapse FRAP assay images of DNAPTP6 dynamics in cells or not
Description
-
Relase date
2023-07-20
Updated date
-
License
CC BY
Kind
Image data based on Experiment
Number of Datasets
5 ( Image datasets: 5, Quantitative data datasets: 0 )
Size of Datasets
1.1 GB ( Image datasets: 1.1 GB, Quantitative data datasets: 0 bytes )

Organism(s)
Mus musculus
Strain(s)
C57BL/6J
Cell lines(s)
CCL-131
Gene symbol(s)
NA
Protein name(s)
NA

Datatype
-
Molecular Function (MF)
ribonucleoprotein complex binding
Biological Process (BP)
Cellular Component (CC)
Biological Imaging Method
FRAP, time lapse microscopy
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
-

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


Dataset List of 294-Asamitsu-DNAPTP6Dyn

#
Dataset ID
Kind
Size
4D View
SSBD:OMERO
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# 10789
Datast ID Fig4B_DNAPTP6
Dataset Kind Image data
Dataset Size 518.5 MB
4D view
SSBD:OMERO
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# 10790
Dataset Kind Image data
Dataset Size 159.8 MB
4D view
SSBD:OMERO
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# 10791
Datast ID Fig4B_DNAPTP6+rG4
Dataset Kind Image data
Dataset Size 159.8 MB
4D view
SSBD:OMERO
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# 10792
Dataset Kind Image data
Dataset Size 337.1 MB
4D view
SSBD:OMERO
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# 10793
Dataset Kind Image data
Dataset Size 1.2 MB
4D view
SSBD:OMERO
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