KUROYANAGI Hidehito

写真a

Title

Professor

Researcher Number(JSPS Kakenhi)

30323702

Date of Birth

1970

Laboratory Address

1076 Kiyuna, Ginowan, Okinawa 901-2720, Japan

Mail Address

E-mail address

Laboratory Phone number

+81-98-894-5457

Homepage URL

https://biochem.med.u-ryukyu.ac.jp/en/

4 9 5

Current Affiliation Organization 【 display / non-display

  • Duty   University of the Ryukyus   Professor  

  • Concurrently   University of the Ryukyus   Professor  

University 【 display / non-display

  • 1989.04
    -
    1994.03

    The University of Tokyo   Faculty of Science   Graduated

Graduate School 【 display / non-display

  • 1994.04
    -
    1996.03

    The University of Tokyo  Graduate School, Division of Science  Master's Course  Completed

  • 1996.04
    -
    1999.03

    The University of Tokyo  Graduate School, Division of Science  Doctor's Course  Completed

Academic degree 【 display / non-display

  • The University of Tokyo -  PhD in Science

External Career 【 display / non-display

  • 1997.04
    -
    1999.03

     

  • 1999.04
    -
    2000.03

     

  • 2000.04
    -
    2003.08

    Tokyo Medical and Dental University, Assistant Professor  

  • 2003.09
    -
    2008.03

    Tokyo Medical and Dental University, Junior Associate Professor  

  • 2008.04
    -
    2012.03

    Tokyo Medical and Dental University, Associate Professor  

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Affiliated academic organizations 【 display / non-display

  •  
     
     
     

    The RNA Society 

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    Genetics Society of America 

  • 2022.04
    -
    2024.03
     

    The RNA Society of Japan 

Research Interests 【 display / non-display

  • Molecular Biology

  • transcriptome

  • model organism

  • gene expression

  • development

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Research Areas 【 display / non-display

  • Life Science / Molecular biology

Published Papers 【 display / non-display

  • UNC5B is an isoform-dependent target for ectodomain shedding.

    Kotaro Sugimoto, Eichi Watabe, Mio Takuma, Kaname Nagahara, Toshinori Sawano, Mihoko Kajita, Junichi Takagi, Hidehito Kuroyanagi, Kyoko Shirakabe

    The Journal of Biochemistry ( Oxford University Press )    mvaf043   2025.07 [ Peer Review Accepted ]

    Type of publication: Research paper (scientific journal)

  • Cytoplasmic mutant RBM20 causes arrhythmogenicity in murine atria.

    Kensuke Ihara, Satoshi Iwamiya, Masaki Ikuta, Yurie Soejima, Yuichi Hiraoka, Atsushi Nakano, Susumu Minamisawa, Tetsushi Furukawa, Hidehito Kuroyanagi, Tetsuo Sasano

    Journal of Molecular and Cellular Cardiology ( Elsevier Ltd. )  205 ( August 2025 ) 1 - 12   2025.06 [ Peer Review Accepted ]

    Type of publication: Research paper (scientific journal)

  • Profiling of RBM20-Regulated CaMKIIδ Splice Variants Across the Heart, Skeletal Muscle, and Olfactory Bulbs.

    Yui Maeda, Yuri Yamasu, Hidehito Kuroyanagi

    Genes to Cells ( John Wiley & Sons, Inc. )  30 ( 3 ) e70021   2025.05 [ Peer Review Accepted ]

    Type of publication: Research paper (scientific journal)

     View Summary

    Calcium/calmodulin-dependent protein kinase IIδ (CaMKIIδ), encoded by the Camk2d gene, plays key regulatory roles in various Ca2+-regulated cellular processes. Extensive alternative splicing of the Camk2d gene generates multiple CaMKIIδ splice variants that exhibit differential roles. Despite significant advances in understanding the functions of CaMKIIδ, the full repertoire of Camk2d splice variants in a variety of tissues and their distinct roles in physiological and pathological contexts remain incompletely characterized due to the complex nature of multiple alternative splicing events. Here, we conducted long-read amplicon sequencing to investigate the murine Camk2d splice variants in the heart, skeletal muscle, and olfactory bulbs and show that Camk2d mRNAs in the heart and skeletal muscle have shorter 3'UTRs. Our results in this study suggest that a key regulator of Camk2d splicing, RNA-binding motif protein 20 (RBM20), whose gain-of-function mutations cause dilated cardiomyopathy, is crucial for the expression of heart-specific splice variants. Olfactory bulbs specifically express novel splice variants that utilize a mutually exclusive exon 6B and/or an alternative polyadenylation site in a novel exon 17.5 in an RBM20-inependent manner. The tissue-specific repertoire of CaMKIIδ splice variants and their aberrant expression in disease model animals will help in understanding their roles in physiological and pathological contexts.

  • Alternative splicing of a single exon causes a major impact on the affinity of Caenorhabditis elegans tropomyosin isoforms for actin filaments.

    Shoichiro Ono, Eichi Watabe, Keita Morisaki, Kanako Ono, Hidehito Kuroyanagi

    Frontiers in Cell and Developmental Biology ( Frontiers Media S.A. )  11   1208913   2023.09 [ Peer Review Accepted ]

    Type of publication: Research paper (scientific journal)

     View Summary

    Tropomyosin is generally known as an actin-binding protein that regulates actomyosin interaction and actin filament stability. In metazoans, multiple tropomyosin isoforms are expressed, and some of them are involved in generating subpopulations of actin cytoskeleton in an isoform-specific manner. However, functions of many tropomyosin isoforms remain unknown. Here, we report identification of a novel alternative exon in the #ICaenorhabditis elegans#IR tropomyosin gene and characterization of the effects of alternative splicing on the properties of tropomyosin isoforms. Previous studies have reported six tropomyosin isoforms encoded by the #IC. elegans lev-11#IR tropomyosin gene. We identified a seventh isoform, LEV-11U, that contained a novel alternative exon, exon 7c (E7c). LEV-11U is a low-molecular-weight tropomyosin isoform that differs from LEV-11T only at the exon 7-encoded region. #IIn silico#IR analyses indicated that the E7c-encoded peptide sequence was unfavorable for coiled-coil formation and distinct from other tropomyosin isoforms in the pattern of electrostatic surface potentials. #IIn vitro#IR, LEV-11U bound poorly to actin filaments, whereas LEV-11T bound to actin filaments in a saturable manner. When these isoforms were transgenically expressed in the #IC. elegans#IR striated muscle, LEV-11U was present in the diffuse cytoplasm with tendency to form aggregates, whereas LEV-11T co-localized with sarcomeric actin filaments. Worms with a mutation in E7c showed reduced motility and brood size, suggesting that this exon is important for the optimal health. These results indicate that alternative splicing of a single exon can produce biochemically diverged tropomyosin isoforms and suggest that a tropomyosin isoform with poor actin affinity has a novel biological function.

  • Simultaneous measurement of nascent transcriptome and translatome using 4-thiouridine metabolic RNA labeling and translating ribosome affinity purification.

    Hirotatsu Imai, Daisuke Utsumi, Hidetsugu Torihara, Kenzo Takahashi, Hidehito Kuroyanagi, Akio Yamashita

    Nucleic Acids Research ( Oxford University Press )  51 ( 14 ) e76   2023.06 [ Peer Review Accepted ]

    Type of publication: Research paper (scientific journal)

     View Summary

    Regulation of gene expression in response to various biological processes, including extracellular stimulation and environmental adaptation requires nascent RNA synthesis and translation. Analysis of the coordinated regulation of dynamic RNA synthesis and translation is required to determine functional protein production. However, reliable methods for the simultaneous measurement of nascent RNA synthesis and translation at the gene level are limited. Here, we developed a novel method for the simultaneous assessment of nascent RNA synthesis and translation by combining 4-thiouridine (4sU) metabolic RNA labeling and translating ribosome affinity purification (TRAP) using a monoclonal antibody against evolutionarily conserved ribosomal P-stalk proteins. The P-stalk-mediated TRAP (P-TRAP) technique recovered endogenous translating ribosomes, allowing easy translatome analysis of various eukaryotes. We validated this method in mammalian cells by demonstrating that acute unfolded protein response (UPR) in the endoplasmic reticulum (ER) induces dynamic reprogramming of nascent RNA synthesis and translation. Our nascent P-TRAP (nP-TRAP) method may serve as a simple and powerful tool for analyzing the coordinated regulation of transcription and translation of individual genes in various eukaryotes.

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Books 【 display / non-display

Other Papers 【 display / non-display

  • New approaches to decipher pre-mRNA splicing codes

    Hidehito Kuroyanagi

    Seikagaku   82 ( 5 ) 402 - 411   2010  [Refereed]

     

    PubMed

  • Visualization of alternative splicing events in vivo.

    Hidehito Kuroyanagi

    Tanpakushitu Kakusan Koso   54 ( 16 ) 2044 - 2048   2009.12  [Refereed]

     

    PubMed

  • Structure, expression and functions of receptor-type protein tyrosine phosphatase RPTP-BK in central nervous system

    Hidehito Kuroyanagi, Masatoshi Tagawa, Takuji Shirasawa

    Tanpakushitu Kakusan Koso   43 ( 8 ) 1162 - 1168   1998.06  [Refereed]

     

    PubMed

Presentations 【 display / non-display

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Grant-in-Aid for Scientific Research 【 display / non-display

  • Elucidation of pathogenesis mechanisms and exploration of therapeutic strategies using mouse models of dilated cardiomyopathy

    Challenging research (sprout)

    Project Year: 2023.06  -  2025.03 

    Investigator(s): KUROYANAGI Hidehito 

    Direct: 5,000,000 (YEN)  Overheads: 1,500,000 (YEN)  Total: 6,500,000 (YEN)

  • Grant-in-Aid for Scientific Research on Innovative Areas

    Project Year: 2020.10  -  2022.03 

    Direct: 7,800,000 (YEN)  Overheads: 2,340,000 (YEN)  Total: 10,140,000 (YEN)

  • Functional Analysis of RBM20 Whose Mutation Causes Dilated Cardiomyopathy

    Challenging research (sprout)

    Project Year: 2020.07  -  2023.03 

    Investigator(s): KUROYANAGI Hidehito 

    Direct: 5,000,000 (YEN)  Overheads: 1,500,000 (YEN)  Total: 6,500,000 (YEN)

  • Tissue-specific pre-mRNA processing in living animals

    Grant-in-Aid for Scientific Research(B)

    Project Year: 2020.04  -  2023.03 

    Investigator(s): KUROYANAGI Hidehito 

    Direct: 13,700,000 (YEN)  Overheads: 4,110,000 (YEN)  Total: 17,810,000 (YEN)

  • Grant-in-Aid for Scientific Research(C)

    Project Year: 2020.04  -  2023.03 

    Direct: 3,300,000 (YEN)  Overheads: 4,290,000 (YEN)  Total: 990,000 (YEN)

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Social Activity 【 display / non-display

  • 2025.08
     
     

  • 2025.04
    -
    2025.07

  • Special Lecture & Lab Exercise in Okinawa AMICUS International Junior High School

    Okinawa AMICUS International Junior High School 

    2024.09
     
     

  • Ninufa-Bushi Seminar

    University of the Ryukyus  The 5th Ninufa-Bushi Seminar in the University of the Ryukyus 

    2023.08
     
     

  • Ninufa-Bushi Seminar

    University of the Ryukyus  The 4th Ninufa-Bushi Seminar in the University of the Ryukyus 

    2022.08
     
     

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Media Coverage 【 display / non-display

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