Updated on 2021/09/21

写真a

 
HIBINO Emi
 
Organization
Graduate School of Pharmaceutical Sciences Department of Basic Medicinal Sciences Structural Biology Designated assistant professor
Title
Designated assistant professor
Contact information
メールアドレス

Degree 1

  1. 薬科学 ( 2017.3   京都大学 ) 

Research Interests 5

  1. intrinsically disordered proteins

  2. protein interaction

  3. Alzheimer's disease

  4. p53

  5. NMR

Research Areas 3

  1. Life Science / Biophysics

  2. Life Science / Pharmaceutical analytical chemistry and physicochemistry

  3. Life Science / Biophysics

Research History 4

  1. Nagoya University   graduate School of Pharmaceutical Science   Designated assistant professor

    2020.6

  2. Shiga University of Medical Science   Molecular Neuroscience Research Center

    2020.6

  3. Shiga University of Medical Science   Designated assistant professor

    2017.4 - 2020.5

      More details

    Country:Japan

  4. Shiga University of Medical Science   Molecular Neuroscience Research Center   Designated assistant professor

    2017.4 - 2020.5

Education 3

  1. 京都大学大学院   薬学研究科

    2011.4 - 2017.3

  2. Kyoto University   Graduate School, Division of Pharmaceutical Sciences

    2013.4 - 2017.3

      More details

    Country: Japan

  3. Kyoto University   Faculty of Pharmaceutical Sciences

    2007.4 - 2011.3

Professional Memberships 7

  1. 日本生化学会

  2. 日本蛋白質科学会

  3. 日本生物物理学会

  4. 日本核磁気共鳴学会

  5. PROTEIN SCIENCE SOCIETY OF JAPAN

  6. THE BIOPHYSICAL SOCIETY OF JAPAN

  7. THE JAPANESE BIOCHEMICAL SOCIETY

▼display all

 

Papers 10

  1. Extracellular Release of ILEI/FAM3C and Amyloid-β Is Associated with the Activation of Distinct Synapse Subpopulations

    Masaki Nakano, Yachiyo Mitsuishi, Lei Liu, Naoki Watanabe, Emi Hibino, Saori Hata, Takashi Saito, Takaomi C. Saido, Shigeo Murayama, Kensaku Kasuga, Takeshi Ikeuchi, Toshiharu Suzuki, Masaki Nishimura

    Journal of Alzheimer's Disease   Vol. 80 ( 1 ) page: 1 - 16   2021.1

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:IOS Press  

    Background: Brain amyloid-β (Aβ) peptide is released into the interstitial fluid (ISF) in a neuronal activity-dependent manner, and Aβ deposition in Alzheimer’s disease (AD) is linked to baseline neuronal activity. Although the intrinsic mechanism for Aβ generation remains to be elucidated, interleukin-like epithelial-mesenchymal transition inducer (ILEI) is a candidate for an endogenous Aβ suppressor. Objective: This study aimed to access the mechanism underlying ILEI secretion and its effect on Aβ production in the brain. Methods: ILEI and Aβ levels in the cerebral cortex were monitored using a newly developed ILEI-specific ELISA and in vivo microdialysis in mutant human Aβ precursor protein-knockin mice. ILEI levels in autopsied brains and cerebrospinal fluid (CSF) were measured using ELISA. Results: Extracellular release of ILEI and Aβ was dependent on neuronal activation and specifically on tetanus toxin-sensitive exocytosis of synaptic vesicles. However, simultaneous monitoring of extracellular ILEI and Aβ revealed that a spontaneous fluctuation of ILEI levels appeared to inversely mirror that of Aβ levels. Selective activation and inhibition of synaptic receptors differentially altered these levels. The evoked activation of AMPA-type receptors resulted in opposing changes to ILEI and Aβ levels. Brain ILEI levels were selectively decreased in AD. CSF ILEI concentration correlated with that of Aβ and were reduced in AD and mild cognitive impairment. Conclusion: ILEI and Aβ are released from distinct subpopulations of synaptic terminals in an activity-dependent manner, and ILEI negatively regulates Aβ production in specific synapse types. CSF ILEI might represent a surrogate marker for the accumulation of brain Aβ.

    DOI: 10.3233/jad-201174

    Scopus

    PubMed

  2. FAM3C in Alzheimer's disease. A risk-related molecule and potential therapeutic target. Reviewed

    Nishimura M, Watanabe N, Mitsuishi Y, Hibino E, Nakano M, Liu L, Sugi T

    Neuroscience of Dementia     page: in press   2020

     More details

    Language:English  

  3. A novel mode of interaction between intrinsically disordered proteins Reviewed

    Emi Hibino, Masaru Hoshino

    Biophysics and Physicobiology   Vol. in press ( 0 ) page: 86 - 93   2020

     More details

    Authorship:Lead author   Publishing type:Research paper (scientific journal)   Publisher:Biophysical Society of Japan  

    DOI: 10.2142/biophysico.bsj-2020012

    Web of Science

    PubMed

    CiNii Article

  4. Lipid class composition of membrane and raft fractions from brains of individuals with Alzheimer's disease. Reviewed International journal

    Akihiro Kawatsuki, Shin-Ya Morita, Naoki Watanabe, Emi Hibino, Yachiyo Mitsuishi, Takuma Sugi, Shigeo Murayama, Masaki Nishimura

    Biochemistry and biophysics reports   Vol. 20 ( 100704 ) page: 100704 - 100704   2019.12

     More details

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

    Perturbation of the homeostasis of brain membrane lipids has been implicated in the pathomechanism of Alzheimer's disease (AD). The ε4 allele of the apolipoprotein E gene (APOE) confers an increased risk, in a dosage-dependent manner, for brain amyloid-β accumulation and the development of sporadic AD. An effect of the APOE genotype on brain lipid homeostasis may underlie the AD risk associated with the ε4 allele. In this research, we examined an effect of APOE ε4 on the lipid class composition of crude membranes and raft-enriched fractions of brains. We applied enzymatic reaction-based methods for the quantification of phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, phosphatidic acid, and sphingomyelin. Our results indicate that brain lipid class composition was neither significantly altered in AD subjects nor affected by the presence of the APOE ε4 allele.

    DOI: 10.1016/j.bbrep.2019.100704

    Scopus

    PubMed

  5. 大脳皮質におけるILEI/FAM3CおよびAβの間質液への分泌様式に関する比較検討 Reviewed

    中野 将希, 三ツ石 弥千代, 渡邊 直希, 日比野 絵美, 斉藤 貴志, 西道 隆臣, 鈴木 利治, 西村 正樹

    Dementia Japan   Vol. 33 ( 4 ) page: 514 - 514   2019.10

     More details

    Language:Japanese   Publishing type:Research paper (scientific journal)   Publisher:(一社)日本認知症学会  

  6. Novel Interaction Mechanism between the Intrinsically Disordered Proteins Invited Reviewed

    Emi Hibino, Masaru Hoshino

    Seibutsu Butsuri   Vol. 59 ( 4 ) page: 202 - 204   2019.7

     More details

    Language:Japanese   Publishing type:Research paper (scientific journal)   Publisher:The Biophysical Society of Japan General Incorporated Association  

    DOI: 10.2142/biophys.59.202

    CiNii Article

  7. Identification of heteromolecular binding sites in transcription factors Sp1 and TAF4 using high-resolution nuclear magnetic resonance spectroscopy Reviewed

    Emi Hibino, Rintaro Inoue, Masaaki Sugiyama, Jun Kuwahara, Katsumi Matsuzaki, Masaru Hoshino

    PROTEIN SCIENCE   Vol. 26 ( 11 ) page: 2280 - 2290   2017.11

     More details

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

    The expression of eukaryotic genes is precisely controlled by interactions between general transcriptional factors and promoter-specific transcriptional activators. The fourth element of TATA-box binding protein-associated factor (TAF4), an essential subunit of the general transcription factor TFIID, serves as a coactivator for various promoter-specific transcriptional regulators. Interactions between TAF4 and site-specific transcriptional activators, such as Sp1, are important for regulating the expression levels of genes of interest. However, only limited information is available on the molecular mechanisms underlying the interactions between these transcriptional regulatory proteins. We herein analyzed the interaction between the transcriptional factors Sp1 and TAF4 using high-resolution solution nuclear magnetic resonance spectroscopy. We found that four glutamine-rich (Q-rich) regions in TAF4 were largely disordered under nearly physiological conditions. Among them, the first Q-rich region in TAF4 was essential for the interaction with another Q-rich region in the Sp1 molecule, most of which was largely disordered. The residues responsible for this interaction were specific and highly localized in a defined region within a range of 20-30 residues. Nevertheless, a detailed analysis of C-13-chemical shift values suggested that no significant conformational change occurred upon binding. These results indicate a prominent and exceptional binding mode for intrinsically disordered proteins other than the well-accepted concept of coupled folding and binding."

    DOI: 10.1002/pro.3287

    Web of Science

    Scopus

    PubMed

  8. Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4 Reviewed

    Emi Hibino, Rintaro Inoue, Masaaki Sugiyama, Jun Kuwahara, Katsumi Matsuzaki, Masaru Hoshino

    PROTEIN SCIENCE   Vol. 25 ( 11 ) page: 2006 - 2017   2016.11

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:WILEY-BLACKWELL  

    The expression of eukaryotic genes is precisely controlled by specific interactions between general transcription initiation factors and gene-specific transcriptional activators. The general transcription factor TFIID, which plays an essential role in mediating transcriptional activation, is a multisubunit complex comprising the TATA box-binding protein (TBP) and multiple TBP-associated factors (TAFs). On the other hand, biochemical and genetic approaches have shown that the promoter-specific transcriptional activator Sp1 has the ability to interact with one of the components of TFIID, the TBP-associated factor TAF4. We herein report the structural details of the glutamine-rich domains (Q-domains) of Sp1 and TAF4 using circular dichroism (CD) and heteronuclear magnetic resonance (NMR) spectroscopy. We found that the two Q-domains of Sp1 and four Q-domains of TAF4 were disordered under physiological conditions. We also quantitatively analyzed the interaction between the Q-domains of Sp1 and TAF4 by NMR and surface plasmon resonance, and detected a weak but specific association between them. Nevertheless, a detailed analysis of CD spectra suggested that any significant conformational change did not occur concomitantly with this association, at least at the level of the overall secondary structure. These results may represent a prominent and exceptional binding mode for the IDPs, which are not categorized in a well-accepted concept of "coupled folding and binding."

    DOI: 10.1002/pro.3013

    Web of Science

    Scopus

    PubMed

  9. Glutamine-rich activation domain of transcription factor Sp1-biochemical activity and structure

    Kuwahara Jun, Uwatoko Chisana, Hibino Emi, Matsuzaki Katsumi, Hoshino Masaru

    PROTEIN SCIENCE   Vol. 24   page: 312 - 312   2015.10

     More details

  10. Interaction between isolated transcriptional activation domains of Sp1 revealed by heteronuclear magnetic resonance Reviewed

    Naoko Hiramatsu, Emi Hibino, Katsumi Matsuzaki, Jun Kuwahara, Masaru Hoshino

    PROTEIN SCIENCE   Vol. 21 ( 10 ) page: 1481 - 1488   2012.10

     More details

    Language:English   Publishing type:Research paper (scientific journal)   Publisher:WILEY-BLACKWELL  

    The promoter-specific transcription factor Sp1 is expressed ubiquitously, and plays a primary role in the regulation of the expression of many genes. Domains A and B located in the N-terminal half of the protein are characterized by glutamine-rich (Q-rich) sequences. These Q-rich domains have been shown to be involved in the interaction between Sp1 and different classes of nuclear proteins, such as TATA-binding protein associated factors. Furthermore, the self-association of Sp1 via Q-rich domains is also important for the regulation of transcriptional activity. It has been considered that an Sp1 molecule bound to a distal GC-box synergistically interacts with another Sp1 molecule at a proximal binding site. Although the formation of multimers via Q-rich domains seems functionally important for Sp1, little is known about the structural and physicochemical nature of the interaction between Q-rich domains. We analyzed the structural details of isolated glutamine-rich B (QB) domains of Sp1 by circular dichroism (CD), analytical ultracentrifugation, and heteronuclear magnetic resonance spectroscopy (NMR). We found the isolated QB domains to be disordered under all conditions examined. Nevertheless, a detailed analysis of NMR spectra clearly indicated interaction between the domains. In particular, the C-terminal half was responsible for the self-association. Furthermore, analytical ultracentrifugation demonstrated weak but significant interaction between isolated QB domains. The self-association between QB domains would be responsible, at least in part, for the formation of multimers by full-length Sp1 molecules that has been proposed to occur during transcriptional activation.

    DOI: 10.1002/pro.2137

    Web of Science

    Scopus

    PubMed

▼display all

MISC 2

  1. Announcing the call for the Special Issue on “The Australian Society for Biophysics (ASB) – 2021 Meeting”

    Charles Cranfield, Donna Whelan, Charles Cox, Keith Shearwin, Joshua Ho, Toby Allen, Risa Shibuya, Emi Hibino, Kumiko Hayashi, Cristobal dos Remedios, Amy Li

    Biophysical Reviews   Vol. 13 ( 4 ) page: 1 - 2   2021.6

     More details

    Language:English   Publisher:Springer Science and Business Media LLC  

    DOI: 10.1007/s12551-021-00813-w

    Scopus

    PubMed

    Other Link: https://link.springer.com/article/10.1007/s12551-021-00813-w/fulltext.html

  2. Glutamine-rich activation domain of transcription factor Sp1-biochemical activity and structure

    Jun Kuwahara, Chisana Uwatoko, Emi Hibino, Katsumi Matsuzaki, Masaru Hoshino

    PROTEIN SCIENCE   Vol. 24   page: 312 - 312   2015.10

     More details

    Language:English   Publishing type:Research paper, summary (international conference)   Publisher:WILEY-BLACKWELL  

    Web of Science

Presentations 15

  1. Active center of Aβ production repressor ILEI/FAM3C

    ○Emi Hibino, Masaki Nishimura

    The 58th Annual Meeting of the Biophysical Society of Japan  2020.9.16 

     More details

    Event date: 2020.9

    Language:English   Presentation type:Poster presentation  

  2. The interaction between transcription factors Sp1 and TAF4 via the intrinsically disordered regions. International conference

    The 9th SKO Symposium Program 

     More details

    Event date: 2015.11

    Language:English   Presentation type:Oral presentation (general)  

    Country:Korea, Republic of  

  3. 転写因子Sp1とTAF4の天然変性領域を介した相互作用 Invited

    日比野 絵美, 井上 倫太郎, 杉山 正明, 桑原 淳, 松崎 勝巳, 星野 大

    第52回日本生物物理学会年会 

     More details

    Event date: 2014.9

    Language:English   Presentation type:Oral presentation (invited, special)  

    Venue:札幌   Country:Japan  

  4. 転写因子Sp1とTAF4の天然変性領域を介した相互作用の解析

    日比野 絵美, 桑原 淳, 松崎 勝巳, 星野 大

    第13回日本蛋白質科学会年会  

     More details

    Event date: 2013.6

    Language:Japanese   Presentation type:Poster presentation  

    Venue:鳥取   Country:Japan  

  5. グリチルリチンとタイト結合裏打ちタンパク質ZO1-PDZ1ドメインとの結合解析

    日比野絵美, 久田美咲, 合田名都子, 天野剛志, 廣明秀一

    令和2年度 生物物理中部支部講演会  2021.3 

     More details

    Language:English   Presentation type:Oral presentation (general)  

  6. グリチルリチンのタイト結合裏打ちタンパク質ZO1 PDZ1ドメインへの結合構造の解析

    日比野絵美, 久田美咲, 合田名都子, 天野剛志, 廣明秀一

    日本薬学会第141年会  2021.3 

     More details

    Language:English   Presentation type:Oral presentation (general)  

  7. ILEI/FAM3C Suppresses Amyloid-β Generation by a Unique Mechanism International conference

    Emi Hibino

    24th MNRC International symposium  2018.9 

     More details

    Language:English   Presentation type:Symposium, workshop panel (nominated)  

  8. Risk for Alzheimer's disease and ILEI/FAM3C that suppresses amyloid-β generation by a unique mechanism

    ◯Emi Hibino, Naoki Watanabe, Masaki Nishimura

    The 91st Annual Meeting of the Japanese Biochemical Society  2018.9 

     More details

    Language:Japanese   Presentation type:Symposium, workshop panel (public)  

  9. Structure-based analysis of ILEI/FAM3C activity to inhibit Aβ generation

    ◯Emi Hibino, Masatake Sugita, Yachiyo Mitsuishi, Naoki Watanabe, Masaki Nakano, Takuma Sugi, Masaki Nishimura

    The 56th Annual Meeting of The Biophysical Society of Japan  2018.9 

     More details

    Language:English   Presentation type:Oral presentation (general)  

  10. ILEI/FAM3C represses Aβ production: structural and functional properties

    Emi Hibino

    ConBio2017  2017.12 

     More details

    Language:English   Presentation type:Poster presentation  

  11. 天然変性領域間の相互作用の物理化学的解析

    日比野 絵美

    蛋白質異常凝集研究会  2017.12 

     More details

    Language:Japanese   Presentation type:Oral presentation (general)  

  12. Aβ産生抑制タンパク質ILEIの構造解析に基づく機能メカニズムの検討

    日比野 絵美

    第36回日本認知症学会学術集会  2017.11 

     More details

    Language:Japanese   Presentation type:Poster presentation  

  13. The interaction between transcription factors Sp1 and TAF4 via the intrinsically disordered regions. International conference

    ◯Emi Hibino, Rintaro Inoue, Masaaki Sugiyama, Jun Kuwahara, Katsumi Matsuzaki, Masaru Hoshino

    The 9th SKO Symposium Program  2015.11 

     More details

    Language:English   Presentation type:Oral presentation (general)  

  14. 転写因子Sp1とTAF4の天然変性領域を介した相互作用 Invited

    日比野 絵美, 井上 倫太郎, 杉山 正明, 桑原 淳, 松崎 勝巳, 星野 大

    第52回日本生物物理学会年会  2014.9 

     More details

    Language:English   Presentation type:Oral presentation (invited, special)  

  15. 転写因子Sp1とTAF4の天然変性領域を介した相互作用の解析

    日比野 絵美, 桑原 淳, 松崎 勝巳, 星野 大

    第13回日本蛋白質科学会年会  2013.6 

     More details

    Language:Japanese   Presentation type:Poster presentation  

▼display all

KAKENHI (Grants-in-Aid for Scientific Research) 4

  1. がん抑制タンパク質p53の機能喪失につながる新規機構解明

    2021 - 2022.3

    公益財団法人 愛知県がん研究振興会  がんその他の悪性新生物研究助成金 

  2. アミロイドβタンパク質産生を特異的に抑制する新たな機序の解析

    Grant number:18K14883  2018.4 - 2021.3

    科学研究費補助金 

    日比野絵美

      More details

    Authorship:Principal investigator 

  3. ILEIとPresenilin-1との結合構造解析に基づくアルツハイマー病分子治療薬の設計

    2018.4 - 2019.3

    滋賀医科大学  学長裁量経費(若手萌芽研究) 

    日比野 絵美

      More details

    Authorship:Principal investigator  Grant type:Competitive

  4. ILEIとγセクレターゼ複合体との結合構造解析に基づくアルツハイマー病分子治療薬の設計

    2017.4 - 2018.3

    滋賀医科大学  学長裁量経費(若手萌芽研究) 

    日比野 絵美

      More details

    Authorship:Principal investigator  Grant type:Competitive

 

Teaching Experience (Off-campus) 1

  1. 生理学

    京都文化医療専門学校)

 

Academic Activities 2

  1. 第3回滋賀ジュニアリサーチグラント成果発表会

    Role(s):Review, evaluation

    株式会社リバネス  2020.2

     More details

    Type:Competition, symposium, etc. 

  2. サイエンスキャッスル2019関西大会

    Role(s):Review, evaluation

    株式会社リバネス  2019.12

     More details

    Type:Competition, symposium, etc.