HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Institute for Genetic Medicine >
Peer-reviewed Journal Articles, etc >

LncRNA-dependent nuclear stress bodies promote intron retention through SR protein phosphorylation

Files in This Item:
EMBOJ-2019-102729R1_Merged_PDF.pdf13.4 MBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/79022

Title: LncRNA-dependent nuclear stress bodies promote intron retention through SR protein phosphorylation
Authors: Ninomiya, Kensuke Browse this author →KAKEN DB
Adachi, Shungo Browse this author
Natsume, Tohru Browse this author →KAKEN DB
Iwakiri, Junichi Browse this author →KAKEN DB
Terai, Goro Browse this author
Asai, Kiyoshi Browse this author →KAKEN DB
Hirose, Tetsuro Browse this author →KAKEN DB
Keywords: intron retention
noncoding RNA
nuclear stress bodies
phosphorylation
splicing factors
Issue Date: 3-Feb-2020
Publisher: John Wiley & Sons
Journal Title: EMBO Journal
Volume: 39
Issue: 23
Start Page: e102729
Publisher DOI: 10.15252/embj.2019102729
Abstract: A number of long noncoding RNAs (lncRNAs) are induced in response to specific stresses to construct membrane-less nuclear bodies; however, their function remains poorly understood. Here, we report the role of nuclear stress bodies (nSBs) formed on highly repetitive satellite III (HSATIII) lncRNAs derived from primate-specific satellite III repeats upon thermal stress exposure. A transcriptomic analysis revealed that depletion of HSATIII lncRNAs, resulting in elimination of nSBs, promoted splicing of 533 retained introns during thermal stress recovery. A HSATIII-Comprehensive identification of RNA-binding proteins by mass spectrometry (ChIRP-MS) analysis identified multiple splicing factors in nSBs, including serine and arginine-rich pre-mRNA splicing factors (SRSFs), the phosphorylation states of which affect splicing patterns. SRSFs are rapidly de-phosphorylated upon thermal stress exposure. During stress recovery, CDC like kinase 1 (CLK1) was recruited to nSBs and accelerated the re-phosphorylation of SRSF9, thereby promoting target intron retention. Our findings suggest that HSATIII-dependent nSBs serve as a conditional platform for phosphorylation of SRSFs by CLK1 to promote the rapid adaptation of gene expression through intron retention following thermal stress exposure.
Rights: This is the peer reviewed version of the following article: The EMBO Journal: 39(3): e102729., which has been published in final form at https://doi.org/10.15252/embj.2019102729. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.
Type: article (author version)
URI: http://hdl.handle.net/2115/79022
Appears in Collections:遺伝子病制御研究所 (Institute for Genetic Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 廣瀬 哲郎

Export metadata:

OAI-PMH ( junii2 , jpcoar_1.0 )

MathJax is now OFF:


 

 - Hokkaido University