IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v8y2017i1d10.1038_ncomms15100.html
   My bibliography  Save this article

An intermolecular FRET sensor detects the dynamics of T cell receptor clustering

Author

Listed:
  • Yuanqing Ma

    (EMBL Australia Node in Single Molecule Science, School of Medical Sciences, University of New South Wales
    ARC Centre of Excellence in Advanced Molecular Imaging, University of New South Wales)

  • Elvis Pandzic

    (EMBL Australia Node in Single Molecule Science, School of Medical Sciences, University of New South Wales
    ARC Centre of Excellence in Advanced Molecular Imaging, University of New South Wales)

  • Philip R. Nicovich

    (EMBL Australia Node in Single Molecule Science, School of Medical Sciences, University of New South Wales
    ARC Centre of Excellence in Advanced Molecular Imaging, University of New South Wales)

  • Yui Yamamoto

    (EMBL Australia Node in Single Molecule Science, School of Medical Sciences, University of New South Wales
    ARC Centre of Excellence in Advanced Molecular Imaging, University of New South Wales)

  • Joanna Kwiatek

    (EMBL Australia Node in Single Molecule Science, School of Medical Sciences, University of New South Wales
    ARC Centre of Excellence in Advanced Molecular Imaging, University of New South Wales)

  • Sophie V. Pageon

    (EMBL Australia Node in Single Molecule Science, School of Medical Sciences, University of New South Wales
    ARC Centre of Excellence in Advanced Molecular Imaging, University of New South Wales)

  • Aleš Benda

    (Biomedical Imaging Facility, Lowy Cancer Research Centre, University of New South Wales)

  • Jérémie Rossy

    (EMBL Australia Node in Single Molecule Science, School of Medical Sciences, University of New South Wales
    ARC Centre of Excellence in Advanced Molecular Imaging, University of New South Wales)

  • Katharina Gaus

    (EMBL Australia Node in Single Molecule Science, School of Medical Sciences, University of New South Wales
    ARC Centre of Excellence in Advanced Molecular Imaging, University of New South Wales)

Abstract

Clustering of the T-cell receptor (TCR) is thought to initiate downstream signalling. However, the detection of protein clustering with high spatial and temporal resolution remains challenging. Here we establish a Förster resonance energy transfer (FRET) sensor, named CliF, which reports intermolecular associations of neighbouring proteins in live cells. A key advantage of the single-chain FRET sensor is that it can be combined with image correlation spectroscopy (ICS), single-particle tracking (SPT) and fluorescence lifetime imaging microscopy (FLIM). We test the sensor with a light-sensitive actuator that induces protein aggregation upon radiation with blue light. When applied to T cells, the sensor reveals that TCR triggering increases the number of dense TCR–CD3 clusters. Further, we find a correlation between cluster movement within the immunological synapse and cluster density. In conclusion, we develop a sensor that allows us to map the dynamics of protein clustering in live T cells.

Suggested Citation

  • Yuanqing Ma & Elvis Pandzic & Philip R. Nicovich & Yui Yamamoto & Joanna Kwiatek & Sophie V. Pageon & Aleš Benda & Jérémie Rossy & Katharina Gaus, 2017. "An intermolecular FRET sensor detects the dynamics of T cell receptor clustering," Nature Communications, Nature, vol. 8(1), pages 1-11, April.
  • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15100
    DOI: 10.1038/ncomms15100
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms15100
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/ncomms15100?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. Darren B. McAffee & Mark K. O’Dair & Jenny J. Lin & Shalini T. Low-Nam & Kiera B. Wilhelm & Sungi Kim & Shumpei Morita & Jay T. Groves, 2022. "Discrete LAT condensates encode antigen information from single pMHC:TCR binding events," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    2. Sorosh Amiri & Camelia Muresan & Xingbo Shang & Clotilde Huet-Calderwood & Martin A. Schwartz & David A. Calderwood & Michael Murrell, 2023. "Intracellular tension sensor reveals mechanical anisotropy of the actin cytoskeleton," Nature Communications, Nature, vol. 14(1), pages 1-15, 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_ncomms15100. 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.