IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v8y2017i1d10.1038_s41467-017-02050-w.html
   My bibliography  Save this article

NDP52 activates nuclear myosin VI to enhance RNA polymerase II transcription

Author

Listed:
  • Natalia Fili

    (University of Kent)

  • Yukti Hari-Gupta

    (University of Kent)

  • Ália dos Santos

    (University of Kent)

  • Alexander Cook

    (University of Kent)

  • Simon Poland

    (King’s College London)

  • Simon M. Ameer-Beg

    (King’s College London)

  • Maddy Parsons

    (King’s College London)

  • Christopher P. Toseland

    (University of Kent)

Abstract

Myosin VI (MVI) has been found to be overexpressed in ovarian, breast and prostate cancers. Moreover, it has been shown to play a role in regulating cell proliferation and migration, and to interact with RNA Polymerase II (RNAPII). Here, we find that backfolding of MVI regulates its ability to bind DNA and that a putative transcription co-activator NDP52 relieves the auto-inhibition of MVI to enable DNA binding. Additionally, we show that the MVI–NDP52 complex binds RNAPII, which is critical for transcription, and that depletion of NDP52 or MVI reduces steady-state mRNA levels. Lastly, we demonstrate that MVI directly interacts with nuclear receptors to drive expression of target genes, thereby suggesting a link to cell proliferation and migration. Overall, we suggest MVI may function as an auxiliary motor to drive transcription.

Suggested Citation

  • Natalia Fili & Yukti Hari-Gupta & Ália dos Santos & Alexander Cook & Simon Poland & Simon M. Ameer-Beg & Maddy Parsons & Christopher P. Toseland, 2017. "NDP52 activates nuclear myosin VI to enhance RNA polymerase II transcription," Nature Communications, Nature, vol. 8(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-02050-w
    DOI: 10.1038/s41467-017-02050-w
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-017-02050-w
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-017-02050-w?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. Louise Canon & Carlos Kikuti & Vicente J. Planelles-Herrero & Tianming Lin & Franck Mayeux & Helena Sirkia & Young il Lee & Leila Heidsieck & Léonid Velikovsky & Amandine David & Xiaoyan Liu & Dihia M, 2023. "How myosin VI traps its off-state, is activated and dimerizes," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    2. Jie Shi & Kristine Hauschulte & Ivan Mikicic & Srijana Maharjan & Valerie Arz & Tina Strauch & Jan B. Heidelberger & Jonas V. Schaefer & Birgit Dreier & Andreas Plückthun & Petra Beli & Helle D. Ulric, 2023. "Nuclear myosin VI maintains replication fork stability," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    3. Ália dos Santos & Daniel E. Rollins & Yukti Hari-Gupta & Hannah McArthur & Mingxue Du & Sabrina Yong Zi Ru & Kseniia Pidlisna & Ane Stranger & Faeeza Lorgat & Danielle Lambert & Ian Brown & Kevin Howl, 2023. "Autophagy receptor NDP52 alters DNA conformation to modulate RNA polymerase II transcription," Nature Communications, Nature, vol. 14(1), pages 1-24, December.
    4. Janeska J. Jonge & Andreas Graw & Vasileios Kargas & Christopher Batters & Antonino F. Montanarella & Tom O’Loughlin & Chloe Johnson & Susan D. Arden & Alan J. Warren & Michael A. Geeves & John Kendri, 2024. "Motor domain phosphorylation increases nucleotide exchange and turns MYO6 into a faster and stronger motor," Nature Communications, Nature, vol. 15(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:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-02050-w. 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.