Updated on 2025/06/26

Information

 

写真a

 
NAKAYAMA SUZUNE
 
Organization
Faculty of Medical Sciences Department of Molecular Biology Assistant Professor
School of Medicine Department of Medicine(Concurrent)
Graduate School of Systems Life Sciences Department of Systems Life Sciences(Concurrent)
Title
Assistant Professor

Degree

  • 理学博士 ( 2024.3 Kyushu University )

Research History

  • Kyushu University Faculty of Medicine Assistant Professor (In charge of graduate school) Ph.D.

    2024.4 - Present

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    Country:Japan

Education

  • Kyushu University   システム生命科学府  

    - 2024.3

Research Interests・Research Keywords

  • Research theme: p97ATPase-mediated biogenesis of organelles

    Keyword: Golgi

    Research period: 2018.4 - Present

Papers

  • VCIP135 associates with both the N- and C-terminal regions of p97 ATPase

    Nakayama, S; Kondo, H

    JOURNAL OF BIOLOGICAL CHEMISTRY   300 ( 1 )   105540   2024.1   ISSN:00219258 eISSN:1083-351X

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    Language:English   Publisher:Journal of Biological Chemistry  

    Two distinct p97ATPase-mediated membrane fusion pathways are required for Golgi and endoplasmic reticulum (ER) biogenesis, namely, the p97/p47 pathway and the p97/p37 pathway. p97 (VCP)/p47 complex-interacting protein p135 (VCIP135) is necessary for both of these pathways. Although VCIP135 is known to form a complex with p97 in the cytosol, the role of this complex in Golgi and ER biogenesis has remained unclear. In this study, we demonstrated that VCIP135 has two distinct p97-binding sites at its N- and C-terminal regions. In particular, the C-terminal binding site includes the SHP motif, which is also found in other p97-binding proteins, such as p47, p37, and Ufd1. We also clarified that VCIP135 binds to both the N- and C-terminal regions of p97; that is, the N- and C-terminal binding sites in VCIP135 interact with the C- and N-terminal regions of p97, respectively. These two interactions within the complex are synchronously controlled by the nucleotide state of p97. We next generated VCIP135 mutants lacking each of the p97-binding sites to investigate their functions in living cells and clarified that VCIP135 is involved in Golgi and ER biogenesis through its two distinct interactions with p97. VCIP135 is hence a unique p97-binding protein that functions by interacting with both the N-and C-terminal regions of p97, which strongly suggests that it plays crucial roles in p97-mediated events.

    DOI: 10.1016/j.jbc.2023.105540

    Web of Science

    Scopus

    PubMed

Professional Memberships

  • Japanese society of molecular biology

    2020.4 - Present

Research Projects

  • オルガネラ形成に必要なp97ATPase膜融合におけるVCIP135の作用機序

    Grant number:24K23189  2024.7 - 2026.3

    Grants-in-Aid for Scientific Research  Grant-in-Aid for Research Activity Start-up

    中山 鈴音

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    Grant type:Scientific research funding

    オルガネラ膜融合は複雑な多段階反応から構成されているが、各段階反応の機能的連結にについて未だ不明である。
    申請者はこの程新たに、p97/p47膜融合経路における膜係留複合体関連因子VCIP135を見出した。本研究では生化学的手法に加え、in vitro beads凝集法、in vivo mitochondria aggregation assay、試験管内ゴルジ体再構成系といった申請者の研究室に独自の手法を用いたVCIP135の膜係留複合体への作用機序の解析および膜係留複合体とSNARE複合体の機能的連結の解析を通して、複雑な多段階反応からなるオルガネラ膜融合全体の機序の解明を目指している。

    CiNii Research