Updated on 2026/06/04

Information

 

写真a

 
YAMASHITA SHUNICHI
 
Organization
Faculty of Medical Sciences Department of Basic Medicine Assistant Professor
School of Medicine Department of Medicine（Concurrent）
Title
Assistant Professor
Contact information
メールアドレス
Tel
0926426089
Profile
細胞内小器官の動態および制御機構の解明を通して、様々な疾患と細胞内小器官の恒常性維持との関係性を明らかにする。
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External link

Research Areas

  • Life Science / Molecular biology

Degree

  • Ph.D.

Research History

  • Kyushu University Graduate School of Medical Sciences Assistant Professor 

    2024.4 - Present

  • 新潟大学大学院医歯学総合研究科・助教   

Research Interests・Research Keywords

  • Research theme： Autophagy

    Keyword： Autophagy

    Research period： 2026

  • Research theme： mitochondria

    Keyword： mitochondria

    Research period： 2026

  • Research theme： mitophagy

    Keyword： mitophagy

    Research period： 2026

  • Research theme： peroxisome

    Keyword： peroxisome

    Research period： 2026

  • Research theme： ペキソファジー

    Keyword： ペキソファジー

    Research period： 2026

  • Research theme： オートファジー

    Keyword： オートファジー

    Research period： 2026

  • Research theme： Pexophagy

    Keyword： Pexophagy

    Research period： 2026

  • Research theme： Molecular mechanisms and physiological roles of organellophagy

    Keyword： mitochondria, peroxisome, autophagy, mitophagy, pexophagy

    Research period： 2007.6

Awards

  • JB Reviewer Award

    2024.11   The Japanese Biochemical Society  

  • 新潟大学学長賞

    2017.5   新潟大学  

  • 柿内三郎記念奨励研究賞

    2011.5   日本生化学会  

Papers

  • Mutant-specific dysfunction of RHOBTB2 impairs mitochondrial function and Na+/K+-ATPase levels in a cell model. Reviewed International journal

    Sachiko Miyamoto, Shun-Ichi Yamashita, Hazrat Belal, Mitsuhiro Kato, Tomotake Kanki, Hirotomo Saitsu

    Biochimica et biophysica acta. Molecular cell research   1873 ( 3 )   120103 - 120103   2026.3   （ ISSN:0167-4889 eISSN:1879-2596 ）

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：Biochimica Et Biophysica Acta Molecular Cell Research  

    RHOBTB2 is an atypical Rho GTPase implicated in developmental and epileptic encephalopathy, yet its pathogenic mechanisms remain poorly understood. In this study, we established a cell model in which RHOBTB2 expression was induced by a doxycycline-inducible system to investigate the functional consequences of disease-associated RHOBTB2 mutants. Protein expression and localization analyses revealed mutant-specific behaviors: GTPase-domain mutants such as D92H and W217C showed no significant difference in RHOBTB2 protein levels compared with WT, while hotspot mutants (R461H, R485C, R489Q) exhibited increased RHOBTB2 protein levels with nuclear and mitochondrial accumulation. RNA-seq analysis revealed that cells expressing each mutant showed distinct transcriptomic changes. Notably, induction of the R489Q mutant caused a robust downregulation of ion channel-related genes, supporting its potential role in disrupting neuronal excitability. Furthermore, expression of mutant RHOBTB2 led to a reduction in Na+/K+-ATPase protein levels via a lysosome-dependent degradation pathway. This effect was particularly prominent in GTPase-domain mutants (D92H and W217C), suggesting a mechanistic link between mutant RHOBTB2 and impaired ion homeostasis. Moreover, the R489Q and W217C mutants impaired mitochondrial respiration, whereas other mutants did not show detectable mitochondrial dysfunction. Importantly, the Y284D cancer-associated mutant did not share these phenotypes, highlighting the diversity of functional outcomes across different mutation sites. The observed dysregulation of ion transport pathways and mitochondrial impairment in some mutants may represent key mechanisms underlying seizure susceptibility and other neurological manifestations in RHOBTB2-associated encephalopathies.

    DOI： 10.1016/j.bbamcr.2025.120103

    Web of Science

    Scopus

    PubMed

  • Mitochondrial fission during mitophagy requires both inner and outer mitofissins. Reviewed International journal

    Kentaro Furukawa, Tatsuro Maruyama, Yuji Sakai, Shun-Ichi Yamashita, Keiichi Inoue, Tomoyuki Fukuda, Nobuo N Noda, Tomotake Kanki

    EMBO reports   27 ( 4 )   853 - 872   2026.2   （ ISSN:1469-221X eISSN:1469-3178 ）

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：EMBO Reports  

    Mitophagy maintains mitochondrial homeostasis through the selective degradation of damaged or excess mitochondria. Recently, we identified mitofissin/Atg44, a mitochondrial intermembrane space-resident fission factor, which directly acts on lipid membranes and drives mitochondrial fission required for mitophagy in yeast. However, it remains unclear whether mitofissin is sufficient for mitophagy-associated mitochondrial fission and whether other factors act from outside mitochondria. Here, we identify a mitochondrial outer membrane-resident mitofissin-like microprotein required for mitophagy, and we name it mitofissin 2/Mfi2 based on the following results. Overexpression of an N-terminal Atg44-like region of Mfi2 induces mitochondrial fragmentation and partially restores mitophagy in atg44Δ cells. Mfi2 binds to lipid membranes and mediates membrane fission in a cardiolipin-dependent manner in vitro, demonstrating its intrinsic mitofissin activity. Coarse-grained molecular dynamics simulations further support the stable interaction of Mfi2 with cardiolipin-containing bilayers. Genetic analyses reveal that Mfi2 and the dynamin-related protein Dnm1 independently facilitate mitochondrial fission during mitophagy. Thus, Atg44 and Mfi2, two mitofissins with distinct localizations, are required for mitophagy-associated mitochondrial fission.

    DOI： 10.1038/s44319-025-00689-x

    Web of Science

    Scopus

    PubMed

  • The mitophagy receptors BNIP3 and NIX mediate tight attachment and expansion of the isolation membrane to mitochondria. Reviewed International journal

    Shun-Ichi Yamashita, Ritsuko Arai, Hiroshi Hada, Benjamin Scott Padman, Michael Lazarou, David C Chan, Tomotake Kanki, Satoshi Waguri

    The Journal of cell biology   224 ( 7 )   2025.7   （ ISSN:0021-9525 eISSN:1540-8140 ）

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    Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Journal of Cell Biology  

    BNIP3 and NIX are the main receptors for mitophagy, but their mechanisms of action remain elusive. Here, we used correlative light EM (CLEM) and electron tomography to reveal the tight attachment of isolation membranes (IMs) to mitochondrial protrusions, often connected with ER via thin tubular and/or linear structures. In BNIP3/NIX-double knockout (DKO) HeLa cells, the ULK1 complex and nascent IM formed on mitochondria, but the IM did not expand. Artificial tethering of LC3B to mitochondria induced mitophagy that was equally efficient in DKO cells and WT cells. BNIP3 and NIX accumulated at the segregated mitochondrial protrusions via binding with LC3 through their LIR motifs but did not require dimer formation. Finally, the average distance between the IM and the mitochondrial surface in receptor-mediated mitophagy was significantly smaller than that in ubiquitin-mediated mitophagy. Collectively, these results indicate that BNIP3 and NIX are required for the tight attachment and expansion of the IM along the mitochondrial surface during mitophagy.

    DOI： 10.1083/jcb.202408166

    Web of Science

    Scopus

    PubMed

  • Atg44/Mdi1/mitofissin facilitates Dnm1-mediated mitochondrial fission Reviewed

    Kentaro Furukawa, Manabu Hayatsu, Kentaro Okuyama, Tomoyuki Fukuda, Shun-Ichi Yamashita, Keiichi Inoue, Shinsuke Shibata, Tomotake Kanki

    Autophagy   20 ( 10 )   2314 - 2322   2024.10   （ ISSN:1554-8627 eISSN:1554-8635 ）

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：Informa UK Limited  

    Mitochondria undergo fission and fusion, and their coordinated balance is crucial for maintaining mitochondrial homeostasis. In yeast, the dynamin-related protein Dnm1 is a mitochondrial fission factor acting from outside the mitochondria. We recently reported the mitochondrial intermembrane space protein Atg44/mitofissin/Mdi1/Mco8 as a novel fission factor, but the relationship between Atg44 and Dnm1 remains elusive. Here, we show that Atg44 is required to complete Dnm1-mediated mitochondrial fission under homeostatic conditions. Atg44-deficient cells often exhibit enlarged mitochondria with accumulated Dnm1 and rosary-like mitochondria with Dnm1 foci at constriction sites. These mitochondrial constriction sites retain the continuity of both the outer and inner membranes within an extremely confined space, indicating that Dnm1 is unable to complete mitochondrial fission without Atg44. Moreover, accumulated Atg44 proteins are observed at mitochondrial constriction sites. These findings suggest that Atg44 and Dnm1 cooperatively execute mitochondrial fission from inside and outside the mitochondria, respectively. Abbreviation: ATG: autophagy related; CLEM: correlative light and electron microscopy; EM: electron microscopy; ER: endoplasmic reticulum; ERMES: endoplasmic reticulum-mitochondria encounter structure; GA: glutaraldehyde; GFP: green fluorescent protein; GTP: guanosine triphosphate: IMM: inner mitochondrial membrane; IMS: intermembrane space; OMM: outer mitochondrial membrane; PB: phosphate buffer; PBS: phosphate-buffered saline; PFA: paraformaldehyde; RFP: red fluorescent protein; WT: wild type.

    DOI： 10.1080/15548627.2024.2360345

    Web of Science

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  • Comprehensive analysis of non-selective and selective autophagy in yeast <i>atg</i> mutants and characterization of autophagic activity in the absence of the Atg8 conjugation system Reviewed

    Tamara Ginevskaia, Aleksei Innokentev, Kentaro Furukawa, Tomoyuki Fukuda, Manabu Hayatsu, Shun-ichi Yamashita, Keiichi Inoue, Shinsuke Shibata, Tomotake Kanki

    The Journal of Biochemistry   176 ( 3 )   217 - 227   2024.6   （ ISSN:0021-924X eISSN:1756-2651 ）

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：Oxford University Press (OUP)  

    Abstract

    Most autophagy-related genes, or ATG genes, have been identified in studies using budding yeast. Although the functions of the ATG genes are well understood, the contributions of individual genes to non-selective and various types of selective autophagy remain to be fully elucidated. In this study, we quantified the activity of non-selective autophagy, the cytoplasm-to-vacuole targeting (Cvt) pathway, mitophagy, endoplasmic reticulum (ER)-phagy, and pexophagy in all Saccharomyces cerevisiae atg mutants. Among the mutants of the core autophagy genes considered essential for autophagy, the atg13 mutant and mutants of the genes involved in the two ubiquitin-like conjugation systems retained residual autophagic functionality. In particular, mutants of the Atg8 ubiquitin-like conjugation system (the Atg8 system) exhibited substantial levels of non-selective autophagy, the Cvt pathway, and pexophagy, although mitophagy and ER-phagy were undetectable. Atg8-system mutants also displayed intravacuolar vesicles resembling autophagic bodies, albeit at significantly reduced size and frequency. Thus, our data suggest that membranous sequestration and vacuolar delivery of autophagic cargo can occur in the absence of the Atg8 system. Alongside these findings, the comprehensive analysis conducted here provides valuable datasets for future autophagy research.

    DOI： 10.1093/jb/mvae042

    Web of Science

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  • Mitophagy mediated by BNIP3 and NIX protects against ferroptosis by downregulating mitochondrial reactive oxygen species Reviewed International journal

    @Yamashita SI, @Sugiura Y, @Matsuura Y, @Maeda R, @Inoue K, @Furukawa K, @Fukuda T, @Chan DC, @Kanki T

    Cell Death and Differentiation   2024.3

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    Authorship：Lead author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

    Mitophagy plays an important role in the maintenance of mitochondrial homeostasis and can be categorized into two types: ubiquitin-mediated and receptor-mediated pathways. During receptor-mediated mitophagy, mitophagy receptors facilitate mitophagy by tethering the isolation membrane to mitochondria. Although at least five outer mitochondrial membrane proteins have been identified as mitophagy receptors, their individual contribution and interrelationship remain unclear. Here, we show that HeLa cells lacking BNIP3 and NIX, two of the five receptors, exhibit a complete loss of mitophagy in various conditions. Conversely, cells deficient in the other three receptors show normal mitophagy. Using BNIP3/NIX double knockout (DKO) cells as a model, we reveal that mitophagy deficiency elevates mitochondrial reactive oxygen species (mtROS), which leads to activation of the Nrf2 antioxidant pathway. Notably, BNIP3/NIX DKO cells are highly sensitive to ferroptosis when Nrf2-driven antioxidant enzymes are compromised. Moreover, the sensitivity of BNIP3/NIX DKO cells is fully rescued upon the introduction of wild-type BNIP3 and NIX, but not the mutant forms incapable of facilitating mitophagy. Consequently, our results demonstrate that BNIP3 and NIX-mediated mitophagy plays a role in regulating mtROS levels and protects cells from ferroptosis.

    DOI： 10.1038/s41418-024-01280-y

    PubMed

  • Imeglimin mitigates the accumulation of dysfunctional mitochondria to restore insulin secretion and suppress apoptosis of pancreatic β-cells from db/db mice Reviewed International journal

    @Aoyagi K, @Nishikawa C, @Nakamichi Y, @Yamashita SI, @Kanki T, @Ohara-Imaizumi M.

    Scientific Reports   14 ( 1 )   2024.3   （ eISSN:2045-2322 ）

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

    Abstract

    Mitochondrial dysfunction in pancreatic β-cells leads to impaired glucose-stimulated insulin secretion (GSIS) and type 2 diabetes (T2D), highlighting the importance of autophagic elimination of dysfunctional mitochondria (mitophagy) in mitochondrial quality control (mQC). Imeglimin, a new oral anti-diabetic drug that improves hyperglycemia and GSIS, may enhance mitochondrial activity. However, chronic imeglimin treatment’s effects on mQC in diabetic β-cells are unknown. Here, we compared imeglimin, structurally similar anti-diabetic drug metformin, and insulin for their effects on clearance of dysfunctional mitochondria through mitophagy in pancreatic β-cells from diabetic model db/db mice and mitophagy reporter (CMMR) mice. Pancreatic islets from db/db mice showed aberrant accumulation of dysfunctional mitochondria and excessive production of reactive oxygen species (ROS) along with markedly elevated mitophagy, suggesting that the generation of dysfunctional mitochondria overwhelmed the mitophagic capacity in db/db β-cells. Treatment with imeglimin or insulin, but not metformin, reduced ROS production and the numbers of dysfunctional mitochondria, and normalized mitophagic activity in db/db β-cells. Concomitantly, imeglimin and insulin, but not metformin, restored the secreted insulin level and reduced β-cell apoptosis in db/db mice. In conclusion, imeglimin mitigated accumulation of dysfunctional mitochondria through mitophagy in diabetic mice, and may contribute to preserving β-cell function and effective glycemic control in T2D.

    DOI： 10.1038/s41598-024-56769-w

    Other Link： https://www.nature.com/articles/s41598-024-56769-w

  • Mitophagy Responds to the Environmental Temperature and Regulates Mitochondrial Mass in Adipose Tissues Invited Reviewed

    Shun-ichi Yamashita, Tomotake Kanki

    Advances in Experimental Medicine and Biology   1461   229 - 243   2024   （ ISSN:00652598 ISBN:978-981-97-4586-9 eISSN:2214-8019 ）

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    Authorship：Lead author,　Corresponding author   Language：English   Publishing type：Part of collection (book)   Publisher：Springer Nature Singapore  

    There are at least two types of adipose tissues in the body, defined as brown adipose tissues (BATs) and white adipose tissues (WATs). These tissues comprise brown and white adipocytes, respectively. The adipocytes are commonly endowed with mitochondria, but they have diverse characteristics and roles. Brown adipocytes have abundant mitochondria that contribute to the β-oxidation of fatty acids to produce chemical energy and the production of heat via uncoupling of the mitochondrial membrane potential from ATP synthesis. Alternatively, white adipocytes have fewer mitochondria that contribute to the generation of free fatty acids via lipogenesis by providing key intermediates. Besides the described types of adipocytes, brown-like adipocytes, termed beige adipocytes, are developed in WAT depots during cold exposure. Beige adipocytes also contribute to thermogenesis. Notably, beige adipocytes may transform into white-like adipocytes after the withdrawal of cold exposure. This process is marked by the elimination of mitochondria through the activation of mitochondria autophagy (mitophagy). This review aims to describe the mitophagy that occurs during the beige-to-white transition and discuss recent insights into the molecular mechanisms of this transformation. Additionally, we describe the mitophagy monitoring strategy in adipose tissues using three independent reporter systems and discuss the availabilities and limitations of the method.

    DOI： 10.1007/978-981-97-4584-5_16

    Web of Science

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  • Hva22, a REEP family protein in fission yeast, promotes reticulophagy in collaboration with a receptor protein. Reviewed International journal

    @Fukuda T, @Saigusa T, @Furukawa K, @Inoue K, @Yamashita SI, @Kanki T.

    Autophagy   2023.10

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1080/15548627.2023.2214029

  • The mitochondrial intermembrane space protein mitofissin drives mitochondrial fission required for mitophagy Reviewed International journal

    @Fukuda T, @Furukawa K, @Maruyama T, @Yamashita SI, @Noshiro D, @Song C, @Ogasawara Y, @Okuyama K, @Alam JM, @Hayatsu, M, @Saigusa T, @Inoue K, @Ikeda K, @Takai A, @Chen L, @Lahiri V, @Okada Y, @Shibata S, @Murata K, @Klionsky DJ, @Noda NN, @Kanki T.

    Molecular Cell   2023.6   （ ISSN:1097-2765 ）

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

    DOI： 10.1016/j.molcel.2023.04.022

  • TIM23 facilitates PINK1 activation by safeguarding against OMA1-mediated degradation in damaged mitochondria. Reviewed International journal

    @Akabane S, @Watanabe K, @Kosako H, @Yamashita SI, @Nishino K, @Kato M, @Sekine S, @Kanki T, @Matsuda N, @Endo T, @Oka T.

    Cell Reports   112454 - 112454   2023.5   （ ISSN:2211-1247 ）

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

    DOI： 10.1016/j.celrep.2023.112454

  • Myeloid-associated differentiation marker is an essential host factor for human parechovirus PeV-A3 entry Reviewed International journal

    @Watanabe K, @Oka T, @Takagi H, @Anisimov S, @Yamashita SI, @Katsuragi Y, @Takahashi M, @Higuchi M, @Kanki T, @Saitoh A, @Fujii M

    Nature Communications   14 ( 1 )   2023.3   （ eISSN:2041-1723 ）

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

    Abstract

    Human parechovirus (PeV-A) is an RNA virus that belongs to the family Picornaviridae and it is currently classified into 19 genotypes. PeV-As usually cause mild illness in children and adults. Among the genotypes, PeV-A3 can cause severe diseases in neonates and young infants, resulting in neurological sequelae and death. In this study, we identify the human myeloid-associated differentiation marker (MYADM) as an essential host factor for the entry of six PeV-As (PeV-A1 to PeV-A6), including PeV-A3. The infection of six PeV-As (PeV-A1 to PeV-A6) to human cells is abolished by knocking out the expression of MYADM. Hamster BHK-21 cells are resistant to PeV-A infection, but the expression of human MYADM in BHK-21 confers PeV-A infection and viral production. Furthermore, VP0 capsid protein of PeV-A3 interacts with one extracellular domain of human MYADM on the cell membrane of BHK-21. The identification of MYADM as an essential entry factor for PeV-As infection is expected to advance our understanding of the pathogenesis of PeV-As.

    DOI： 10.1038/s41467-023-37399-8

    Other Link： https://www.nature.com/articles/s41467-023-37399-8

  • A new beta cell-specific mitophagy reporter mouse shows that metabolic stress leads to accumulation of dysfunctional mitochondria despite increased mitophagy Reviewed International journal

    @Aoyagi K, @Yamashita SI, @Akimoto Y, @Nishikawa C, @Nakamichi Y, @Udagawa H, @Abe M, @Sakimura K, @Kanki T, @Ohara-Imaizumi M

    Diabetologia   66 ( 1 )   147 - 162   2023.1   （ ISSN:0012-186X eISSN:1432-0428 ）

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

    DOI： 10.1007/s00125-022-05800-8

    Other Link： https://link.springer.com/article/10.1007/s00125-022-05800-8/fulltext.html

  • Mitophagy reporter mouse analysis reveals increased mitophagy activity in disuse-induced muscle atrophy Reviewed International journal

    @Yamashita SI, @Kyuuma M, @Inoue K, @Hata Y, @Kawada R, @Yamabi M, @Fujii Y, @Sakagami J, @Fukuda T, @Furukawa K, @Tsukamoto S, @Kanki T

    Journal of Cellular Physiology   2021.11

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1002/jcp.30404

  • Fis1 ablation in the male germline disrupts mitochondrial morphology and mitophagy, and arrests spermatid maturation Reviewed International journal

    @Varuzhanyan G, @Ladinsky MS, @Yamashita SI, @Abe M, @Sakimura K, @Kanki T, @Chan DC

    Development   2021.8

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1242/dev.199686

  • The optineurin/TIA1 pathway inhibits aberrant stress granule formation and reduces ubiquitinated TDP-43 Reviewed International journal

    @Kakihana T, @Takahashi M, @Katsuragi Y, @Yamashita SI, @Sango J, @Kanki T, @Onodera O, @Fujii M

    iScience   2021.6

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1016/j.isci.2021.102733

  • MITOL promotes cell survival by degrading Parkin during mitophagy Reviewed International journal

    @Shiiba I, @Takeda K, @Nagashima S, @Ito N, @Tokuyama T, @Yamashita SI, @Kanki T, @Komatsu T, @Urano Y, @Fujikawa Y, @Inatome R, @Yanagi S

    EMBO Reports   2021.3

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.15252/embr.201949097

  • Association and dissociation between the mitochondrial Far complex and Atg32 regulate mitophagy Reviewed International journal

    @Innokentev A, @Furukawa K, @Fukuda T, @Saigusa T, @Inoue K, @Yamashita SI, @Kanki T

    Elife   2020.12

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.7554/eLife.63694

  • Atg43 tethers isolation membranes to mitochondria to promote starvation-induced mitophagy in fission yeast Reviewed International journal

    @Fukuda T, @Ebi Y, @Saigusa T, @Furukawa K, @Yamashita SI, @Inoue K, @Kobayashi D, @Yoshida Y, @Kanki T

    Elife   2020.11

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.7554/eLife.61245

  • FKBP8 LIRL-dependent mitochondrial fragmentation facilitates mitophagy under stress conditions Reviewed International journal

    @Yoo SM, @Yamashita SI, @Kim H, @Na D, @Lee H, @Kim SJ, @Cho DH, @Kanki T, @Jung YK

    FASEB Journal   2020.2

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1096/fj.201901735R

  • Gemcitabine induces Parkin-independent mitophagy through mitochondrial-resident E3 ligase MUL1-mediated stabilization of PINK1 Reviewed International journal

    @Igarashi R, @Yamashita SI, @Yamashita T, @Inoue K, @Fukuda T, @Fukuchi T, @Kanki T

    Scientific Reports   2020.1

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1038/s41598-020-58315-w

  • Glaucoma-Associated Mutations in the Optineurin Gene Have Limited Impact on Parkin-Dependent Mitophagy Reviewed International journal

    @Chernyshova K, @Inoue K, @Yamashita SI, @Fukuchi T, @Kanki T

    Investigative Ophthalmology and Visual Science   2019.8

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1167/iovs.19-27184

  • The PP2A-like Protein Phosphatase Ppg1 and the Far Complex Cooperatively Counteract CK2-Mediated Phosphorylation of Atg32 to Inhibit Mitophagy Reviewed International journal

    @Furukawa K, @Fukuda T, @Yamashita SI, @Saigusa T, @Kurihara Y, @Yoshida Y, @Kirisako H, @Nakatogawa H, @Kanki T

    Cell Reports   2018.6

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1016/j.celrep.2018.05.064

  • Detection of Hypoxia-Induced and Iron Depletion-Induced Mitophagy in Mammalian Cells Reviewed International journal

    @Yamashita SI, @Kanki T

    Methods in Molecular Biology, Mitophagy   2018.5

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1007/7651_2017_19

  • Detection of Iron Depletion- and Hypoxia-induced Mitophagy in Mammalian Cells Reviewed International journal

    @Yamashita SI, @Kanki T

    Methods in Molecular Biology, Mitochondrial Bioenergetics   2018.5

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1007/978-1-4939-7831-1_18

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Books

  • DERMATOLOGY Reviewed

    Shun-ichi Yamashita, Tomotake Kanki（Role：Joint authorMolecular mechanisms of autophagy）

    科学評論社  2024.5 

  • 温度ストレスによる生体応答ダイナミクス Reviewed

    山下俊一（Role：Joint author体温調節におけるミトコンドリア分解の重要性とその分子機構）

    エヌ・ティー・エス  2023.5    （ ISBN:9784860438302 ）

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    Total pages：2, 8, 337, 10p, 図版 21p   Language：Japanese  

    CiNii Books

Presentations

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MISC

  • 2型糖尿病関連SNPとミトコンドリア機能低下との関係性解明による新規疾患発症機序の提唱

    山下 俊一

    医科学応用研究財団研究報告   43   457 - 459   2026.2   （ ISSN:0914-5117 ）

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    Language：Japanese   Publisher：(公財)鈴木謙三記念医科学応用研究財団  

  • 【皮膚における細胞死:病態への関与】オートファジーの分子機構

    山下 俊一, 神吉 智丈

    皮膚科   5 ( 5 )   472 - 478   2024.5   （ ISSN:2436-570X ）

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    Language：Japanese   Publisher：(有)科学評論社  

  • Imeglimin preserves mitochondrial quality control to restore β-cell functions in db/db mice

    青柳共太, 西脇知世乃, 中道洋子, 山下俊一, 神吉智丈, 今泉美佳

    糖尿病(Web)   67 ( Suppl )   2024   （ ISSN:1881-588X ）

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  • 膵β細胞特異的マイトファジーレポーターマウスによって明らかになった糖尿病におけるミトコンドリア品質管理の重要性

    青柳共太, 山下俊一, 神吉智丈, 今泉美佳

    日本生化学会大会(Web)   95th   2022

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  • 膵β細胞特異的マイトファジーレポーターマウスによって明らかになった糖尿病におけるミトコンドリア品質管理の重要性

    青柳共太, 山下俊一, 神吉智丈, 今泉美佳

    糖尿病(Web)   65 ( Suppl )   2022   （ ISSN:1881-588X ）

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  • How autophagy eats large mitochondria: Autophagosome formation coupled with mitochondrial fragmentation Reviewed

    @Shun-ichi Yamashita, @Tomotake Kanki

    2017.5

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    Language：English   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

    DOI： 10.1080/15548627.2017.1291113

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Professional Memberships

  • 日本細胞生物学会

  • 日本分子生物学会

  • 日本ミトコンドリア学会

  • 日本生化学会

Academic Activities

  • Screening of academic papers

    Role(s)： Peer review

    2023

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    Type：Peer review 

    Number of peer-reviewed articles in foreign language journals：5

  • Screening of academic papers

    Role(s)： Peer review

    2022

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    Type：Peer review 

    Number of peer-reviewed articles in foreign language journals：8

Research Projects

  • 哺乳類マイトフィッシンによるミトコンドリア膜切断機構の解析

    Grant number：26K01966  2026.4 - 2029.3

    Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (B)

    山下 俊一

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    Grant type：Scientific research funding

    CiNii Research

  • レセプター依存型マイトファジーにおける膜界面現象の研究

    Grant number：26H01637  2026.4 - 2028.3

    Grants-in-Aid for Scientific Research  Grant-in-Aid for Transformative Research Areas (A)

    山下 俊一

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    Grant type：Scientific research funding

    CiNii Research

  • 2型糖尿病関連SNPとミトコンドリア機能低下との関係性解明による新規疾患発症機序の提唱

    2023 - 2024

    鈴木謙三記念医科学応用研究財団・調査研究助成金

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    Authorship：Principal investigator  Grant type：Contract research

  • Regulation of receptor-mediated mitophagy and its physiological roles

    Grant number：23K23878  2022.4 - 2025.3

    Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (B)

    Kanki Tomotake

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    Grant type：Scientific research funding

    We analyzed BNIP3/NIX_DKO cells as receptor-mediated mitophagy-deficient cells and found that receptor- mediated mitophagy protects cells from ferroptosis by maintaining low levels of mtROS. Furthermore, we revealed that the role of the mitophagy receptors BNIP3 and NIX in mitophagy is to mediate tight attachment and expansion of the isolation membrane to mitochondria.

    CiNii Research

  • Elucidation of the molecular mechanism of the mitophagy contributing to the drug resistance and its application to chemotherapy

    Grant number：22K07207  2022.4 - 2025.3

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

    Yamashita Shun-ichi

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    Grant type：Scientific research funding

    Anticancer drugs are known to induce mitochondrial autophagy (mitophagy). In this study, we aimed to elucidate the molecular mechanism and physiological significance of anticancer drug-induced mitophagy. We demonstrated that BNIP3/NIX, mitophagy receptors, are required for anticancer drug-induced mitophagy. We discovered that cells BNIP3/NIX double knockout cells are highly sensitive to ferroptosis.
    Ultrastructural analysis of mitophagy revealed that the isolation membrane tightly attaches to mitochondria. Furthermore, we demonstrated that the assembly of BNIP3/NIX in between the isolation membrane and mitochondria is essential for the tight attachment.

    CiNii Research

  • 抗がん剤耐性に関与する新奇マイトファジーの分子機構解明と化学療法への応用

    2022 - 2024

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (C)

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    Grant type：Scientific research funding

  • 哺乳類ペルオキシソーム分解の分子機構とその生理的意義に関する研究

    2010 - 2012

    Japan Society for the Promotion of Science  Research Fellowships for Young Scientists

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    Authorship：Principal investigator  Grant type：Joint research

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Class subject

  • 生理学実習

    2025.9 - 2025.10  

  • 人体構造と機能III

    2025.5  

  • 生理学

    2025.4 - 2026.3  

  • 生理学実習

    2024.9 - 2024.10  

  • 生理学

    2024.4 - 2025.3  

  • 人体構造と機能III

    2024.4 - 2024.9   First semester

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Visiting, concurrent, or part-time lecturers at other universities, institutions, etc.

  • 2024  新潟大学大学院医歯学総合研究科  Classification:Affiliate faculty  Domestic/International Classification:Japan