YONEMURA Yoji

写真a

Affiliation

Graduate School of Medicine  Doctorial Course in Medicine  Bioregulatory Medicine  Department of Cell Biology and Morphology

Date of Birth

1983

Research Interests 【 display / non-display

  • Alzheimer's disease

  • タンパク質の局在

Graduating School 【 display / non-display

  • 2005.04
    -
    2009.03

    Waseda University     Graduated

Graduate School 【 display / non-display

  • 2011.04
    -
    2014.03

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

  • 2009.04
    -
    2011.03

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

Studying abroad experiences 【 display / non-display

  • 2015.04
    -
    2019.03

    Leibniz Institute on Aging - Fritz Lipmann Institute (FLI)   Postdoctoral Fellow

  • 2014.04
    -
    2015.03

    Leibniz Institute on Aging - Fritz Lipmann Institute (FLI)   JSPS Research Fellowship for Young Scientists (PD)

Campus Career 【 display / non-display

  • 2025.12
    -
    Now

    Akita University   Graduate School of Medicine   Doctorial Course in Medicine   Bioregulatory Medicine   Department of Cell Biology and Morphology   Assistant Professor  

External Career 【 display / non-display

  • 2025.12
     
     

    Akita University   Graduate School of Medicine   Assistant Professor  

  • 2024.06
    -
    2025.11

    Kobe University   Engineering Biology Research Center  

  • 2019.04
    -
    2024.03

    Doshisha University   Organization for Research Initiatives and Development   Assistant Professor  

  • 2015.04
    -
    2019.03

    Leibniz Institut für Altersforschung, Fritz-Lipmann-Institut (FLI)  

Research Areas 【 display / non-display

  • Life Science / Cell biology

  • Life Science / Cell biology

 

Research Achievements 【 display / non-display

    ◆Original paper【 display / non-display

  • A YIPF5-GOT1A/B complex directs a transcription independent function of ATF6 in ER export

    Paul Cramer , Yoji Yonemura , Laura Behrendt , Aleksandra Marszalek , Mara Sannai , William Durso , Cagatay Günes , Karol Szafranski , Nobuhiro Nakamura , Tornike Nasrashvili , Johanna Mayer , Björn von Eyss, Christoph Kaether

    bioRxiv : the preprint server for biology     2023.12

    Research paper (journal)   International Co-author

    DOI

  • Active Transport by Cytoplasmic Dynein Maintains the Localization of MAP2 in Developing Neurons.

    Yoji Yonemura, Yuri Sakai, Rinaho Nakata, Ayaka Hagita-Tatsumoto, Tomohiro Miyasaka, Hiroaki Misonou

    bioRxiv : the preprint server for biology     2023.04

    Research paper (journal)   Domestic Co-author

    MAP2 has been widely used as a marker of neuronal dendrites because of its extensive restriction in the somatodendritic region of neurons. Despite that, how the precise localization of such a soluble protein is established and maintained against thermal forces and diffusion has been elusive and long remained a mystery in neuroscience. In this study, we aimed to uncover the mechanism behind how MAP2 is retained in the somatodendritic region. Using GFP-tagged MAP2 expressed in cultured hippocampal neurons, we discovered a crucial protein region responsible for the localization of MAP2, the serine/proline-rich (S/P) region. Our pulse-chase live-cell imaging revealed the slow but steady migration of MAP2 toward distal dendrites, which was not observed in a MAP2 mutant lacking the S/P region, indicating that S/P-dependent transport is vital for the proper localization of MAP2. Furthermore, our experiments using an inhibitor of cytoplasmic Dynein, ciliobrevin D, as well as Dynein knockdown, showed that cytoplasmic Dynein is involved in the transport of MAP2 in dendrites. We also found that Dynein complex binds to MAP2 through the S/P region in heterologous cells. Using mathematical modeling based on experimental data, we confirmed that an intermittent active transport mechanism is essential. Thus, we propose that the cytoplasmic Dynein recruits and transports free MAP2 toward distal dendrites, thereby maintaining the precise dendritic localization of MAP2 in neurons. Our findings shed light on the previously unknown mechanism behind MAP2 localization and provide a new direction for soluble protein trafficking research in the field of cell biology of neurons.

    DOI PubMed

  • COPII collar defines the boundary between ER and ER exit site and does not coat cargo containers.

    Olga Shomron, Inbar Nevo-Yassaf, Tamar Aviad, Yakey Yaffe, Eitan Erez Zahavi, Anna Dukhovny, Eran Perlson, Ilya Brodsky, Adva Yeheskel, Metsada Pasmanik-Chor, Anna Mironov, Galina V Beznoussenko, Alexander A Mironov, Ella H Sklan, George H Patterson, Yoji Yonemura, Mara Sannai, Christoph Kaether, Koret Hirschberg

    The Journal of cell biology   220 ( 6 )   2021.06  [Refereed]

    Research paper (journal)   International Co-author

    COPII and COPI mediate the formation of membrane vesicles translocating in opposite directions within the secretory pathway. Live-cell and electron microscopy revealed a novel mode of function for COPII during cargo export from the ER. COPII is recruited to membranes defining the boundary between the ER and ER exit sites, facilitating selective cargo concentration. Using direct observation of living cells, we monitored cargo selection processes, accumulation, and fission of COPII-free ERES membranes. CRISPR/Cas12a tagging, the RUSH system, and pharmaceutical and genetic perturbations of ER-Golgi transport demonstrated that the COPII coat remains bound to the ER-ERES boundary during protein export. Manipulation of the cargo-binding domain in COPII Sec24B prohibits cargo accumulation in ERES. These findings suggest a role for COPII in selecting and concentrating exported cargo rather than coating Golgi-bound carriers. These findings transform our understanding of coat proteins' role in ER-to-Golgi transport.

    DOI PubMed

  • Inhibition of cargo export at ER exit sites and the trans-Golgi network by the secretion inhibitor FLI-06

    Yoji Yonemura, Xiaolin Li, Katja Mueller, Andreas Kraemer, Paul Atigbire, Torben Mentrup, Talitha Feuerhake, Torsten Kroll, Olga Shomron, Richard Nohl, Hans-Dieter Arndt, Christian Hoischen, Peter Hemmerich, Koret Hirschberg, Christoph Kaether

    JOURNAL OF CELL SCIENCE     2016.10  [Refereed]

    Research paper (journal)   International Co-author

    DOI

  • Specific combinations of presenilins and Aph1s affect the substrate specificity and activity of γ-secretase.

    Yoji Yonemura, Eugene Futai, Sosuke Yagishita, Christoph Kaether, Shoichi Ishiura

    Biochemical and biophysical research communications     2016.09  [Refereed]

    Research paper (journal)   International Co-author

    DOI

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

  • Elucidation of the mechanism underlying the somatodendritic specific localization of microtubule associated protein 2 (MAP2)

    Grant-in-Aid for Early-Career Scientists

    Project Year: 2025.04  -  2028.03 

Presentations 【 display / non-display

  • Active transport by cytoplasmic dynein regulates somatodendritic localization of MAP2

    Yoji Yonemura, Yuri Sakai, Tomohiro Miyasaka, Hiroaki Misonou

    第98回日本生化学会大会  (京都)  2025.11  -  2025.11  日本生化学会

  • MAP2の適切な局在化に関与する因子の同定

    米村洋而, 酒井宥璃, 萩田彩香, 中田, 里奈穂, 宮坂知宏, 御園生裕明

    第44回日本神経科学大会 / CJK第1回国際会議  2021.07  -  2021.07 

  • MAP2の局在を決定する領域の同定

    米村洋而, 宮坂知宏, 御園生裕明

    第43回日本神経科学大会  2020.07  -  2020.07 

  • The COPII heterocomplex is a gatekeeper that selects and concentrates transportcompetent cargo in endoplasmic reticulum exit sites

    Koret Hirschberg, Olga Shomron, Inbar Nevo-Yassaf, Eran Perlson, George H. Patterson, Yoji Yonemura, Christoph Kaether

    EMBO Workshop on “ER function in health and disease”  2018.10  -  2018.10 

  • Genome-wide loss- and gain-of-function screens to find novel players in ER-export

    Yoji Yonemura, Laura Behrendt, Mara Sannai, Paul Cramer, Björn von Eyß, Christoph Kaether

    EMBO Workshop on “ER function in health and disease”  2018.10  -  2018.10 

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