IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v5y2014i1d10.1038_ncomms4891.html
   My bibliography  Save this article

Clathrin light chains are required for the gyrating-clathrin recycling pathway and thereby promote cell migration

Author

Listed:
  • Sophia R. Majeed

    (University of California San Francisco
    University of California San Francisco
    University of California San Francisco
    The G.W. Hooper Foundation, University of California San Francisco)

  • Lavanya Vasudevan

    (University of California San Francisco
    University of California San Francisco
    University of California San Francisco
    The G.W. Hooper Foundation, University of California San Francisco)

  • Chih-Ying Chen

    (University of California San Francisco
    University of California San Francisco
    University of California San Francisco
    The G.W. Hooper Foundation, University of California San Francisco)

  • Yi Luo

    (Thomas Jefferson University)

  • Jorge A. Torres

    (University of California San Francisco
    University of California San Francisco
    University of California San Francisco
    The G.W. Hooper Foundation, University of California San Francisco)

  • Timothy M. Evans

    (University of California San Francisco
    University of California San Francisco
    University of California San Francisco
    The G.W. Hooper Foundation, University of California San Francisco)

  • Andrew Sharkey

    (University of Cambridge)

  • Amy B. Foraker

    (University of California San Francisco
    University of California San Francisco
    University of California San Francisco
    The G.W. Hooper Foundation, University of California San Francisco)

  • Nicole M. L. Wong

    (University of California San Francisco
    University of California San Francisco
    University of California San Francisco
    The G.W. Hooper Foundation, University of California San Francisco)

  • Christopher Esk

    (University of California San Francisco
    University of California San Francisco
    University of California San Francisco
    The G.W. Hooper Foundation, University of California San Francisco)

  • Theresa A. Freeman

    (Thomas Jefferson University)

  • Ashley Moffett

    (University of Cambridge)

  • James H. Keen

    (Thomas Jefferson University)

  • Frances M. Brodsky

    (University of California San Francisco
    University of California San Francisco
    University of California San Francisco
    The G.W. Hooper Foundation, University of California San Francisco)

Abstract

The clathrin light chain (CLC) subunits participate in several membrane traffic pathways involving both clathrin and actin, through binding the actin-organizing huntingtin-interacting proteins (Hip). However, CLCs are dispensable for clathrin-mediated endocytosis of many cargoes. Here we observe that CLC depletion affects cell migration through Hip binding and reduces surface expression of β1-integrin by interference with recycling following normal endocytosis of inactive β1-integrin. CLC depletion and expression of a modified CLC also inhibit the appearance of gyrating (G)-clathrin structures, known mediators of rapid recycling of transferrin receptor from endosomes. Expression of the modified CLC reduces β1-integrin and transferrin receptor recycling, as well as cell migration, implicating G-clathrin in these processes. Supporting a physiological role for CLC in migration, the CLCb isoform of CLC is upregulated in migratory human trophoblast cells during uterine invasion. Together, these studies establish CLCs as mediating clathrin–actin interactions needed for recycling by G-clathrin during migration.

Suggested Citation

  • Sophia R. Majeed & Lavanya Vasudevan & Chih-Ying Chen & Yi Luo & Jorge A. Torres & Timothy M. Evans & Andrew Sharkey & Amy B. Foraker & Nicole M. L. Wong & Christopher Esk & Theresa A. Freeman & Ashle, 2014. "Clathrin light chains are required for the gyrating-clathrin recycling pathway and thereby promote cell migration," Nature Communications, Nature, vol. 5(1), pages 1-14, September.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4891
    DOI: 10.1038/ncomms4891
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms4891
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms4891?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
    ---><---

    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:5:y:2014:i:1:d:10.1038_ncomms4891. 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.