Masayuki Sakurai

Masayuki Sakurai
Tokyo University of Science | TUS · Research Institute for Biomedical Sciences

Ph.D.

About

26
Publications
6,571
Reads
How we measure 'reads'
A 'read' is counted each time someone views a publication summary (such as the title, abstract, and list of authors), clicks on a figure, or views or downloads the full-text. Learn more
1,181
Citations
Additional affiliations
April 2018 - present
Tokyo University of Science
Position
  • Professor (Associate)
Description
  • Division of Molecular Pathology, Sakurai Lab. Research on RNA, Cancer, and Inflammation.
April 2010 - March 2018
Wistar Institute
Position
  • Professor (Assistant)
Description
  • ▪ The Wistar Institute in Gene Expression and Regulation Program, Nishikura laboratory. Functions of RNA editing enzyme ADARs in molecular and cellular biology.
April 2006 - March 2010
The University of Tokyo
Position
  • Fellow
Description
  • ▪ The University of Tokyo, Dept. of Integrated Biosciences, Grad. School of Engineering. Transcriptome-wide identification of A-to-I RNA editing with new biochemical method.
Education
April 2003 - March 2006
The University of Tokyo, Department of Frontier Science, Graduate School of Integrated Biosciences
Field of study
  • Molecular Biology
April 2001 - March 2003
The University of Tokyo, Department of Frontier Science, Graduate School of Integrated Biosciences
Field of study
  • Molecular Biology
April 1997 - March 2001
Department of Chemistry and Biotechnology, Faculty of Engineering
Field of study
  • Biochemistry

Publications

Publications (26)
Article
Full-text available
Inosine is an abundant RNA modification in the human transcriptome and is essential for many biological processes by modulating gene expression at the post-transcriptional level. Adenosine deaminases acting on RNA (ADARs) catalyze the hydrolytic deamination of adenosines to inosines (A-to-I editing) in double-stranded regions. We previously establi...
Article
Full-text available
Adenosine-to-inosine (A-to-I) RNA editing is a post-transcriptional processing event involved in diversifying the transcriptome responsible for various biological processes. Although bioinformatic approaches have predicted a number of A-to-I editing sites in cDNAs, the human transcriptome is thought to still harbor large numbers of as-yet-unknown e...
Article
Full-text available
Adenosine deaminases acting on RNA (ADARs) are involved in RNA editing that converts adenosine residues to inosine specifically in double-stranded RNAs. In this study, we investigated the interaction of the RNA editing mechanism with the RNA interference (RNAi) machinery and found that ADAR1 forms a complex with Dicer through direct protein-protein...
Article
Full-text available
Metastasis is a critical event affecting breast cancer patient survival. To identify molecules contributing to the metastatic process, we analysed The Cancer Genome Atlas (TCGA) breast cancer data and identified 41 genes whose expression is inversely correlated with survival. Here we show that GABAA receptor alpha3 (Gabra3), normally exclusively ex...
Article
Full-text available
Inosine (I), a modified base found in the double-stranded regions of RNA in metazoans, has various roles in biological processes by modulating gene expression. Inosine is generated from adenosine (A) catalyzed by ADAR (adenosine deaminase acting on RNA) enzymes in a process called A-to-I RNA editing. As inosine is converted to guanosine (G) by reve...
Article
Full-text available
ADAR1 is involved in adenosine-to-inosine RNA editing. The cytoplasmic ADAR1p150 edits 3’UTR double-stranded RNAs and thereby suppresses induction of interferons. Loss of this ADAR1p150 function underlies the embryonic lethality of Adar1 null mice, pathogenesis of the severe autoimmune disease Aicardi-Goutières syndrome, and the resistance develope...
Article
Full-text available
Adenosine-to-inosine (A-to-I) editing is one of the most prevalent post-transcriptional RNA modifications in metazoan. This reaction is catalyzed by enzymes called adenosine deaminases acting on RNA (ADARs). RNA editing is involved in the regulation of protein function and gene expression. The numerous A-to-I editing sites have been identified in b...
Chapter
Full-text available
RNA editing of adenosines to inosines contributes to a wide range of biological processes by regulating gene expression post-transcriptionally. To understand the effect, accurate mapping of inosines is necessary. The most conventional method to identify an editing site is to compare the cDNA sequence with its corresponding genomic sequence. However...
Article
Full-text available
In addition to adenosine-to-inosine RNA editing activities, ADAR1 has been shown to have various RNA editing independent activities including modulation of RNAi efficacy. We previously reported that ADAR1 forms a heterodimer complex with DICER and facilitates processing of pre-miRNAs to mature miRNAs. In addition to miRNA synthesis, DICER is involv...
Article
Full-text available
Both p150 and p110 isoforms of ADAR1 convert adenosine to inosine in double-stranded RNA (dsRNA). ADAR1p150 suppresses the dsRNA-sensing mechanism that activates MDA5-MAVS-IFN signaling in the cytoplasm. In contrast, the biological function of the ADAR1p110 isoform, which is usually located in the nucleus, is largely unknown. Here, we show that str...
Article
Full-text available
Adenosine deaminases acting on RNA (ADARs) convert adenosine to inosine in double-stranded RNA (dsRNA). Among the three types of mammalian ADARs, ADAR1 has long been recognized as an essential enzyme for normal development. The interferon-inducible ADAR1p150 is involved in immune responses to both exogenous and endogenous triggers, whereas the func...
Data
Supplementary Figures 1-14 and Supplementary Tables 1-2
Article
Full-text available
Inosine (I) is a modified adenosine (A) in RNA. In Metazoa, I is generated by hydrolytic deamination of A, catalyzed by adenosine deaminase acting RNA (ADAR) in a process called A-to-I RNA editing. A-to-I RNA editing affects various biological processes by modulating gene expression. In addition, dysregulation of A-to-I RNA editing results in patho...
Article
Full-text available
Adenosine deaminases acting on RNA (ADARs) are involved in RNA editing that converts adenosine residues to inosine specifically in double-stranded RNAs (dsRNA). This A-to-I RNA editing pathway and the RNA interference (RNAi) pathway seem to interact antagonistically by competing for their common dsRNA substrates. For instance, A-to-I editing of cer...
Article
Full-text available
Adenosine deaminases acting on RNA (ADARs) are involved in RNA editing that converts adenosine residues to inosine specifically in double-stranded RNAs. In this study, we investigated the interaction of the RNA editing mechanism with the RNA interference (RNAi) machinery and found that ADAR1 forms a complex with Dicer through direct protein-protein...
Article
Full-text available
Catalysed by members of the adenosine deaminase acting on RNA (ADAR) family of enzymes, adenosine-to-inosine (A-to-I) editing converts adenosines in RNA molecules to inosines, which are functionally equivalent to guanosines. Recently, global approaches to studying this widely conserved phenomenon have emerged. The use of bioinformatics, high-throug...
Article
Full-text available
Adenosine-to-inosine (A-to-I) RNA editing is a biologically important posttranscriptional processing event involved in the transcriptome diversification. The most conventional method of editing site identification is to compare the cDNA sequence with its corresponding genomic sequence; however, using this method, it is difficult to discriminate bet...
Article
Full-text available
Nematode mitochondria possess extremely truncated tRNAs. Of 22 tRNAs, 20 lack the entire T-arm. The T-arm is necessary for the binding of canonical tRNAs and EF (elongation factor)-Tu (thermo-unstable). The nematode mitochondrial translation system employs two different EF-Tu factors named EF-Tu1 and EF-Tu2. Our previous study showed that nematode...
Article
Full-text available
To understand the decoding property of nematode mitochondrial tRNAs with unusual secondary structures, post-transcriptional modifications at wobble positions of Ascaris suum mitochondrial tRNAs corresponding to two-codon families ending with a purine were analyzed. 5-Carboxymethylaminomethyluridine (cmnm(5)U) was identified at the wobble positions...
Article
Full-text available
Nematode mitochondria expresses two types of extremely truncated tRNAs that are specifically recognized by two distinct elongation factor Tu (EF-Tu) species named EF-Tu1 and EF-Tu2. This is unlike the canonical EF-Tu molecule that participates in the standard protein biosynthesis systems, which basically recognizes all elongator tRNAs. EF-Tu2 speci...
Article
Full-text available
The mitochondria of the nematode Ascaris suum have tRNAs with unusual secondary structures that lack either the T-arm or D-arm found in most other organisms. Of the twenty-two tRNA species present in the mitochondria of A.suum, twenty lack the entire T-arm and two serine tRNAs lack the D-arm. To understand how such unusual tRNAs work in the nematod...
Article
Full-text available
Caenorhabditis elegans mitochondria have two elongation factor (EF)‐Tu species, denoted EF‐Tu1 and EF‐Tu2. Recombinant nematode EF‐Ts purified from Escherichia coli bound both of these molecules and also stimulated the translational activity of EF‐Tu, indicating that the nematode EF‐Ts homolog is a functional EF‐Ts protein of mitochondria. Complexe...
Article
Full-text available
Most of nematode mitochondrial (mt) tRNAs lacking the T arm have 1-methyladenosine (m1A) at position 9. To investigate the effect of m1A, we constructed a nematode Ascaris suum mt tRNA(Met) containing only m1A9 as the modified nucleoside by means of molecular surgery. Although the unmodified A. suum mt Met-tRNA(Met) did not bind to nematode mt EF-T...

Projects

Project (1)
Project
My research interest is the molecular mechanisms and biological functions of RNA modifications and binding proteins. I am mainly working on ADARs and A-to-I editing to reveal new roles in cancer, inflammation, and some severe diseases, including molecular mechanisms/pathways between editing and resultant cellular phenotype. I believe there are more roles for RNA editing than ones we know currently. Also, I am trying to establish a novel method to identify other RNA/DNA modifications with new biochemical reactions such as the ICE-seq I established before. My final aim is to pioneer a new direction that connects nucleic acids modifications and "true" central dogma with new findings and new techniques.