IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v10y2019i1d10.1038_s41467-019-09720-x.html
   My bibliography  Save this article

KIBRA controls exosome secretion via inhibiting the proteasomal degradation of Rab27a

Author

Listed:
  • Lin Song

    (Shandong Provincial Hospital affiliated to Shandong University)

  • Shi Tang

    (Shandong Provincial Hospital affiliated to Shandong University)

  • Xiaolei Han

    (Shandong Provincial Hospital affiliated to Shandong University)

  • Ziying Jiang

    (Shandong Provincial Hospital affiliated to Shandong University)

  • Lingling Dong

    (Dongying People’s Hospital)

  • Cuicui Liu

    (Shandong Provincial Hospital affiliated to Shandong University)

  • Xiaoyan Liang

    (Shandong Provincial Hospital affiliated to Shandong University)

  • Jixin Dong

    (University of Nebraska Medical Center)

  • Chengxuan Qiu

    (Shandong Provincial Hospital affiliated to Shandong University
    Karolinska Institutet-Stockholm University)

  • Yongxiang Wang

    (Shandong Provincial Hospital affiliated to Shandong University)

  • Yifeng Du

    (Shandong Provincial Hospital affiliated to Shandong University)

Abstract

Exosomes are nanosized membrane vesicles released from cells after fusion of multivesicular bodies (MVBs) with the plasma membrane (PM) and play important roles in intercellular communication and numerous biological processes. However, the molecular mechanisms regulating exosome secretion remain poorly understood. Here we identify KIBRA as an adaptor-like protein that stabilizes Rab27a, which in turn controls exosome secretion both in vitro and in vivo. Knockdown or overexpression of KIBRA in neuronal and podocyte cell lines leads to a decrease or increase of exosome secretion, respectively, and KIBRA depletion increases MVB size and number. Comparing protein profiles between KIBRA knockout and wild-type mouse brain showed significantly decreased Rab27a, a small GTPase that regulates MVB-PM docking. Rab27a is stabilized by interacting with KIBRA, which prevents ubiquitination and degradation via the ubiquitin-proteasome pathway. In conclusion, we show that KIBRA controls exosome secretion via inhibiting the proteasomal degradation of Rab27a.

Suggested Citation

  • Lin Song & Shi Tang & Xiaolei Han & Ziying Jiang & Lingling Dong & Cuicui Liu & Xiaoyan Liang & Jixin Dong & Chengxuan Qiu & Yongxiang Wang & Yifeng Du, 2019. "KIBRA controls exosome secretion via inhibiting the proteasomal degradation of Rab27a," Nature Communications, Nature, vol. 10(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-09720-x
    DOI: 10.1038/s41467-019-09720-x
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-019-09720-x
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-019-09720-x?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. Jiaxin Liang & Deyang Yu & Chi Luo & Christopher Bennett & Mark Jedrychowski & Steve P. Gygi & Hans R. Widlund & Pere Puigserver, 2023. "Epigenetic suppression of PGC1α (PPARGC1A) causes collateral sensitivity to HMGCR-inhibitors within BRAF-treatment resistant melanomas," Nature Communications, Nature, vol. 14(1), pages 1-12, 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:10:y:2019:i:1:d:10.1038_s41467-019-09720-x. 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.