IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v6y2015i1d10.1038_ncomms8052.html
   My bibliography  Save this article

JMJD1A is a signal-sensing scaffold that regulates acute chromatin dynamics via SWI/SNF association for thermogenesis

Author

Listed:
  • Yohei Abe

    (Research Center for Advanced Science and Technology (RCAST), The University of Tokyo)

  • Royhan Rozqie

    (Research Center for Advanced Science and Technology (RCAST), The University of Tokyo
    Faculty of Medicine, Gadjah Mada University)

  • Yoshihiro Matsumura

    (Research Center for Advanced Science and Technology (RCAST), The University of Tokyo)

  • Takeshi Kawamura

    (Laboratory for Systems Biology and Medicine, Research Center for Advanced Science and Technology (RCAST), The University of Tokyo
    The Translational Systems Biology and Medicine Initiative, Center for Disease Biology and Integrative Medicine, Faculty of Medicine, University of Tokyo)

  • Ryo Nakaki

    (Research Center for Advanced Science and Technology (RCAST), The University of Tokyo)

  • Yuya Tsurutani

    (Research Center for Advanced Science and Technology (RCAST), The University of Tokyo)

  • Kyoko Tanimura-Inagaki

    (Research Center for Advanced Science and Technology (RCAST), The University of Tokyo)

  • Akira Shiono

    (Research Center for Advanced Science and Technology (RCAST), The University of Tokyo)

  • Kenta Magoori

    (Research Center for Advanced Science and Technology (RCAST), The University of Tokyo
    The Translational Systems Biology and Medicine Initiative, Center for Disease Biology and Integrative Medicine, Faculty of Medicine, University of Tokyo)

  • Kanako Nakamura

    (Research Center for Advanced Science and Technology (RCAST), The University of Tokyo)

  • Shotaro Ogi

    (Research Center for Advanced Science and Technology (RCAST), The University of Tokyo)

  • Shingo Kajimura

    (UCSF Diabetes Center, University of California, San Francisco)

  • Hiroshi Kimura

    (Graduate School of Frontier Biosciences, Osaka University)

  • Toshiya Tanaka

    (Research Center for Advanced Science and Technology (RCAST), The University of Tokyo
    Laboratory for Systems Biology and Medicine, Research Center for Advanced Science and Technology (RCAST), The University of Tokyo
    The Translational Systems Biology and Medicine Initiative, Center for Disease Biology and Integrative Medicine, Faculty of Medicine, University of Tokyo)

  • Kiyoko Fukami

    (Laboratory of Genome and Biosignals, Tokyo University of Pharmacy and Life Science)

  • Timothy F. Osborne

    (Metabolic Disease Program, Sanford-Burnham Medical Research Institute)

  • Tatsuhiko Kodama

    (Laboratory for Systems Biology and Medicine, Research Center for Advanced Science and Technology (RCAST), The University of Tokyo)

  • Hiroyuki Aburatani

    (The Translational Systems Biology and Medicine Initiative, Center for Disease Biology and Integrative Medicine, Faculty of Medicine, University of Tokyo
    Research Center for Advanced Science and Technology (RCAST), The University of Tokyo)

  • Takeshi Inagaki

    (Research Center for Advanced Science and Technology (RCAST), The University of Tokyo
    The Translational Systems Biology and Medicine Initiative, Center for Disease Biology and Integrative Medicine, Faculty of Medicine, University of Tokyo)

  • Juro Sakai

    (Research Center for Advanced Science and Technology (RCAST), The University of Tokyo
    The Translational Systems Biology and Medicine Initiative, Center for Disease Biology and Integrative Medicine, Faculty of Medicine, University of Tokyo)

Abstract

Histone 3 lysine 9 (H3K9) demethylase JMJD1A regulates β-adrenergic-induced systemic metabolism and body weight control. Here we show that JMJD1A is phosphorylated at S265 by protein kinase A (PKA), and this is pivotal to activate the β1-adrenergic receptor gene (Adrb1) and downstream targets including Ucp1 in brown adipocytes (BATs). Phosphorylation of JMJD1A by PKA increases its interaction with the SWI/SNF nucleosome remodelling complex and DNA-bound PPARγ. This complex confers β-adrenergic-induced rapid JMJD1A recruitment to target sites and facilitates long-range chromatin interactions and target gene activation. This rapid gene induction is dependent on S265 phosphorylation but not on demethylation activity. Our results show that JMJD1A has two important roles in regulating hormone-stimulated chromatin dynamics that modulate thermogenesis in BATs. In one role, JMJD1A is recruited to target sites and functions as a cAMP-responsive scaffold that facilitates long-range chromatin interactions, and in the second role, JMJD1A demethylates H3K9 di-methylation.

Suggested Citation

  • Yohei Abe & Royhan Rozqie & Yoshihiro Matsumura & Takeshi Kawamura & Ryo Nakaki & Yuya Tsurutani & Kyoko Tanimura-Inagaki & Akira Shiono & Kenta Magoori & Kanako Nakamura & Shotaro Ogi & Shingo Kajimu, 2015. "JMJD1A is a signal-sensing scaffold that regulates acute chromatin dynamics via SWI/SNF association for thermogenesis," Nature Communications, Nature, vol. 6(1), pages 1-14, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8052
    DOI: 10.1038/ncomms8052
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms8052
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms8052?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Yoshihiro Matsumura & Ryo Ito & Ayumu Yajima & Rei Yamaguchi & Toshiya Tanaka & Takeshi Kawamura & Kenta Magoori & Yohei Abe & Aoi Uchida & Takeshi Yoneshiro & Hiroyuki Hirakawa & Ji Zhang & Makoto Ar, 2021. "Spatiotemporal dynamics of SETD5-containing NCoR–HDAC3 complex determines enhancer activation for adipogenesis," Nature Communications, Nature, vol. 12(1), pages 1-19, December.
    2. Hiroki Takahashi & Ge Yang & Takeshi Yoneshiro & Yohei Abe & Ryo Ito & Chaoran Yang & Junna Nakazono & Mayumi Okamoto-Katsuyama & Aoi Uchida & Makoto Arai & Hitomi Jin & Hyunmi Choi & Myagmar Tumenjar, 2022. "MYPT1-PP1β phosphatase negatively regulates both chromatin landscape and co-activator recruitment for beige adipogenesis," Nature Communications, Nature, vol. 13(1), pages 1-19, December.
    3. Jiahui Du & Yili Liu & Jinrui Sun & Enhui Yao & Jingyi Xu & Xiaolin Wu & Ling Xu & Mingliang Zhou & Guangzheng Yang & Xinquan Jiang, 2024. "ARID1A safeguards the canalization of the cell fate decision during osteoclastogenesis," Nature Communications, Nature, vol. 15(1), pages 1-20, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8052. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.