IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v461y2009i7265d10.1038_nature08448.html
   My bibliography  Save this article

JAK2 phosphorylates histone H3Y41 and excludes HP1α from chromatin

Author

Listed:
  • Mark A. Dawson

    (University of Cambridge, Hills Road, Cambridge CB2 0XY, UK
    Addenbrooke’s Hospital, Hills Road, Cambridge CB2 0QQ, UK)

  • Andrew J. Bannister

    (University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK)

  • Berthold Göttgens

    (University of Cambridge, Hills Road, Cambridge CB2 0XY, UK)

  • Samuel D. Foster

    (University of Cambridge, Hills Road, Cambridge CB2 0XY, UK)

  • Till Bartke

    (University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK)

  • Anthony R. Green

    (University of Cambridge, Hills Road, Cambridge CB2 0XY, UK
    Addenbrooke’s Hospital, Hills Road, Cambridge CB2 0QQ, UK)

  • Tony Kouzarides

    (University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK)

Abstract

JAK2 kinase goes nuclear JAK2 is a non-receptor tyrosine kinase that regulates diverse cellular processes by inducing cytoplasmic signalling cascades. Dawson et al. now report a previously unknown nuclear function for JAK2. Tyrosine phosphorylation of histone H3 by JAK2 can lead to disruption of HP1 α binding to chromatin and changes in gene expression. This finding is of particular interest because JAK2 inhibitors are in clinical trials for the treatment of myeloid leukaemias in which JAK2 is dysregulated.

Suggested Citation

  • Mark A. Dawson & Andrew J. Bannister & Berthold Göttgens & Samuel D. Foster & Till Bartke & Anthony R. Green & Tony Kouzarides, 2009. "JAK2 phosphorylates histone H3Y41 and excludes HP1α from chromatin," Nature, Nature, vol. 461(7265), pages 819-822, October.
  • Handle: RePEc:nat:nature:v:461:y:2009:i:7265:d:10.1038_nature08448
    DOI: 10.1038/nature08448
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature08448
    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/nature08448?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. Hidehiro Itonaga & Adnan K. Mookhtiar & Sarah M. Greenblatt & Fan Liu & Concepcion Martinez & Daniel Bilbao & Masai Rains & Pierre-Jacques Hamard & Jun Sun & Afoma C. Umeano & Stephanie Duffort & Chua, 2024. "Tyrosine phosphorylation of CARM1 promotes its enzymatic activity and alters its target specificity," Nature Communications, Nature, vol. 15(1), pages 1-19, December.
    2. Surbhi Chouhan & Dhivya Sridaran & Cody Weimholt & Jingqin Luo & Tiandao Li & Myles C. Hodgson & Luana N. Santos & Samantha Sommer & Bin Fang & John M. Koomen & Markus Seeliger & Cheng-Kui Qu & Armell, 2024. "SHP2 as a primordial epigenetic enzyme expunges histone H3 pTyr-54 to amend androgen receptor homeostasis," Nature Communications, Nature, vol. 15(1), pages 1-19, 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:461:y:2009:i:7265:d:10.1038_nature08448. 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.