IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v516y2014i7529d10.1038_nature13955.html
   My bibliography  Save this article

TRIM37 is a new histone H2A ubiquitin ligase and breast cancer oncoprotein

Author

Listed:
  • Sanchita Bhatnagar

    (Howard Hughes Medical Institute, University of Massachusetts Medical School
    Programs in Gene Function and Expression and Molecular Medicine, University of Massachusetts Medical School)

  • Claude Gazin

    (CEA/DSV/iRCM/LEFG, Genopole G2, and Université Paris Diderot, 91057 Evry, France)

  • Lynn Chamberlain

    (Howard Hughes Medical Institute, University of Massachusetts Medical School
    Programs in Gene Function and Expression and Molecular Medicine, University of Massachusetts Medical School)

  • Jianhong Ou

    (Programs in Gene Function and Expression and Molecular Medicine, University of Massachusetts Medical School)

  • Xiaochun Zhu

    (Howard Hughes Medical Institute, University of Massachusetts Medical School
    Programs in Gene Function and Expression and Molecular Medicine, University of Massachusetts Medical School)

  • Jogender S. Tushir

    (Boehringer Ingelheim Pharmaceuticals, Inc.)

  • Ching-Man Virbasius

    (Howard Hughes Medical Institute, University of Massachusetts Medical School
    Programs in Gene Function and Expression and Molecular Medicine, University of Massachusetts Medical School)

  • Ling Lin

    (Howard Hughes Medical Institute, University of Massachusetts Medical School
    Programs in Gene Function and Expression and Molecular Medicine, University of Massachusetts Medical School)

  • Lihua J. Zhu

    (Programs in Gene Function and Expression and Molecular Medicine, University of Massachusetts Medical School
    Program in Bioinformatics and Integrative Biology, University of Massachusetts Medical School)

  • Narendra Wajapeyee

    (Yale University School of Medicine)

  • Michael R. Green

    (Howard Hughes Medical Institute, University of Massachusetts Medical School
    Programs in Gene Function and Expression and Molecular Medicine, University of Massachusetts Medical School)

Abstract

The RING finger protein TRIM37 is encoded by a gene that is amplified in certain breast cancers, but its function is unknown; here, it is shown to mono-ubiquitinate histone H2A and repress gene expression, and to function as a breast cancer oncoprotein.

Suggested Citation

  • Sanchita Bhatnagar & Claude Gazin & Lynn Chamberlain & Jianhong Ou & Xiaochun Zhu & Jogender S. Tushir & Ching-Man Virbasius & Ling Lin & Lihua J. Zhu & Narendra Wajapeyee & Michael R. Green, 2014. "TRIM37 is a new histone H2A ubiquitin ligase and breast cancer oncoprotein," Nature, Nature, vol. 516(7529), pages 116-120, December.
    • Handle: RePEc:nat:nature:v:516:y:2014:i:7529:d:10.1038_nature13955
    DOI: 10.1038/nature13955
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature13955
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature13955?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
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

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


    Cited by:

    1. Mitsuaki Fujimoto & Ryosuke Takii & Masaki Matsumoto & Mariko Okada & Keiich I. Nakayama & Ryuichiro Nakato & Katsunori Fujiki & Katsuhiko Shirahige & Akira Nakai, 2022. "HSF1 phosphorylation establishes an active chromatin state via the TRRAP–TIP60 complex and promotes tumorigenesis," Nature Communications, Nature, vol. 13(1), pages 1-18, 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:nature:v:516:y:2014:i:7529:d:10.1038_nature13955. 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.