Updated on 2025/08/08

Information

 

写真a

 
CAI XIAOHAN
 
Organization
Medical Institute of Bioregulation Department of Molecular and Structural Biology Assistant Professor
Title
Assistant Professor
Contact information
メールアドレス

Papers

  • Identification of a molecular resistor that controls UCP1-independent Ca2+cycling thermogenesis in adipose tissue

    Auger, C; Li, M; Fujimoto, M; Ikeda, K; Kajimura, S; O'Leary, TR; Caycedo, MPH; Cai, XH; Oikawa, S; Verkerke, ARP; Shinoda, K; Griffin, PR; Inaba, K; Stimson, RH; Kajimura, S

    CELL METABOLISM   37 ( 6 )   1311 - 1325.e9   2025.6   ISSN:1550-4131 eISSN:1932-7420

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  • Mechanistic characterization of disulfide bond reduction of an ERAD substrate mediated by cooperation between ERdj5 and BiP

    Cai, XH; Ito, S; Noi, K; Inoue, M; Ushioda, R; Kato, Y; Nagata, K; Inaba, K

    JOURNAL OF BIOLOGICAL CHEMISTRY   299 ( 11 )   105274   2023.11   ISSN:00219258 eISSN:1083-351X

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    Language:English   Publisher:Journal of Biological Chemistry  

    Endoplasmic reticulum (ER)-associated degradation (ERAD) is a protein quality control process that eliminates misfolded proteins from the ER. DnaJ homolog subfamily C member 10 (ERdj5) is a protein disulfide isomerase family member that accelerates ERAD by reducing disulfide bonds of aberrant proteins with the help of an ER-resident chaperone BiP. However, the detailed mechanisms by which ERdj5 acts in concert with BiP are poorly understood. In this study, we reconstituted an in vitro system that monitors ERdj5-mediated reduction of disulfide-linked J-chain oligomers, known to be physiological ERAD substrates. Biochemical analyses using purified proteins revealed that J-chain oligomers were reduced to monomers by ERdj5 in a stepwise manner via trimeric and dimeric intermediates, and BiP synergistically enhanced this action in an ATP-dependent manner. Single-molecule observations of ERdj5-catalyzed J-chain disaggregation using high-speed atomic force microscopy, demonstrated the stochastic release of small J-chain oligomers through repeated actions of ERdj5 on peripheral and flexible regions of large J-chain aggregates. Using systematic mutational analyses, ERAD substrate disaggregation mediated by ERdj5 and BiP was dissected at the molecular level.

    DOI: 10.1016/j.jbc.2023.105274

    Web of Science

    Scopus

    PubMed

  • Multiple sub-state structures of SERCA2b reveal conformational overlap at transition steps during the catalytic cycle

    Cell Reports   41 ( 111760 )   2022.12

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    Authorship:Corresponding author   Language:English  

    DOI: https://doi.org/10.1016/j.celrep.2022.111760