RNA G-quadruplex organizes stress granule assembly through DNAPTP6 in neurons

Sefan Asamitsu, Yasushi Yabuki, Kazuya Matsuo, Moe Kawasaki, Yuki Hirose, Gengo Kashiwazaki, Anandhakumar Chandran, Toshikazu Bando, Dan Ohtan Wang, Hiroshi Sugiyama, Norifumi Shioda

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish (US)
Article numbereade2035
JournalScience Advances
Issue number8
StatePublished - Feb 2023

ASJC Scopus subject areas

  • General


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