Researcher Database

（Last updated : 2023-02-01 11:29:00）　

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MANNEN TARO

Department / Course College of Life Sciences Department of Biomedical Sciences

Title / Position Assistant Professor

Academic background
1.	2008/03 Degree Acquisition	│ Kumamoto University Ph.D. in Science
2.	～2008/03	Doctoral Program (2nd Semester) │ Materials and Life Science │ Graduate School of Science and Technology │ Kumamoto University │ Completed
3.	～2005/03	Doctoral Program (1st Semester) │ Natural System │ Graduate School of Science and Technology │ Kumamoto University │ Completed
4.	～2003/03	Department of Biological Sciences │ Faculity of Science │ Kumamoto University │ Graduated

Research activities
1.		The RNA Society
2.		The RNA Society of Japan
3.		The Molecular Biology Society of Japan

Research summary
Characterization of nuclear bodies built around RNAs in cancer cell line 　The mammalian cell nucleus contains nuclear bodies characterized by a distinct set of resident proteins. The nuclear bodies are thought to serve as the sites for biogenesis of various RNA species, the storage and assembly of RNP complexes and the retention of specific RNA species. We discovered that a long noncoding RNA (lncRNA) acts as structural scaffold of the specific nuclear body called paraspeckle, and investigated how the lncRNA acts for the paraspeckle assembly with multiple protein factors. Here, we searched for new nuclear bodies that were built on unidentified RNAs by screening of the “RNase-sensitive nuclear bodies” using 10,432 fluorescence-tagged human full-length (FLJ) cDNA clones. First, we chose 463 FLJ cDNA clones whose fluorescently tagged-protein products were localized in certain nuclear foci. Subsequently, we explored whether the respective nuclear focus was abolished or diffused upon RNase treatment after cell permeabilization. In this screening, we identified seven RNA-binding proteins commonly localized in the Sam68 nuclear body (SNB), which is disrupted by RNase treatment. Knockdown of each SNB component revealed that SNB is composed of two distinct RNase-sensitive substructures, and HNRNPL acts as the adaptor of these two substructures to form intact SNB. HNRNPL utilizes the combination of its RNA recognition motifs to interact with the putative scaffold RNAs of each substructure. One of the substructures can be present as the distinct nuclear body called DBC1 body in certain physiological conditions and the more dynamic another substructure including Sam68 joins to form the intact SNB (Mannen et al., J Cell Biol 2016).

Present specialized field
Molecular biology, Cell biology (Keyword：non-coding RNA, Nuclear bodies, RNA-binding protein, Proteomics, Cancer)

Books
1.	2015	Long noncoding RNAs as structural and functional components of nuclear bodies. │ ,pp.111-132

Papers
1.	2021/09	C9orf72-derived arginine-rich poly-dipeptides impede phase modifiers. │ Nature communications │ 12 (1),pp.5301
2.	2021/09	Distinct RNA polymerase transcripts direct the assembly of phase-separated DBC1 nuclear bodies in different cell lines. │ Molecular biology of the cell │ ,pp.mbcE21020081
3.	2021/06/03	ArcRNAs and the formation of nuclear bodies │ Mammalian Genome │
4.	2021/02	Mechanism of karyopherin-β2 binding and nuclear import of ALS variants FUS(P525L) and FUS(R495X) │ Scientific Reports │ 11,pp.3754
5.	2020/09	Siwi levels reversibly regulate secondary piRISC biogenesis by affecting Ago3 body morphology in Bombyx mori │ The EMBO Journal │ ,pp.e105130
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Academic conference presentation
1.	2019/12/05	Analysis of protein-protein interactions within the DBC1 nuclear bodies built around RNAs in cancer cell line
2.	2019/10/01	Analysis of protein-protein interactions within the Sam68 and DBC1 nuclear bodies built around RNAs in cancer cell line
3.	2019/02/01	Characterization of Sam68 and DBC1 nuclear bodies built around RNAs in cancer cell line
4.	2018/11/06	Analysis of protein-protein interactions within the nuclear bodies built around RNAs in cancer cell line
5.	2017/09/09	The Sam68 nuclear body is composed of two RNase-sensitive substructures joined by the adaptor HNRNPL
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Competitive grants, etc. (exc. KAKENHI)
1.	2017/11/01 ～ 2018/11/30	A comprehensive analysis of protein interactions within the nuclear bodies built around RNAs in specific cancer cell lines │ Research by External Competitive Fund

Subject
1.	英語JP2

E-Mail Address