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Super-resolution microscopy compatible fluorescent probes reveal endogenous glucagon-like peptide-1 receptor distribution and dynamics

Author

Listed:
  • Julia Ast

    (University of Birmingham
    Birmingham Health Partners)

  • Anastasia Arvaniti

    (University of Birmingham
    Birmingham Health Partners)

  • Nicholas H. F. Fine

    (University of Birmingham
    Birmingham Health Partners)

  • Daniela Nasteska

    (University of Birmingham
    Birmingham Health Partners)

  • Fiona B. Ashford

    (University of Birmingham
    Birmingham Health Partners)

  • Zania Stamataki

    (University of Birmingham)

  • Zsombor Koszegi

    (University of Birmingham
    Birmingham Health Partners)

  • Andrea Bacon

    (University of Birmingham)

  • Ben J. Jones

    (Imperial College London)

  • Maria A. Lucey

    (Imperial College London)

  • Shugo Sasaki

    (University of British Columbia)

  • Daniel I. Brierley

    (University College London)

  • Benoit Hastoy

    (University of Oxford)

  • Alejandra Tomas

    (Imperial College London)

  • Giuseppe D’Agostino

    (University of Manchester)

  • Frank Reimann

    (University of Cambridge)

  • Francis C. Lynn

    (University of British Columbia)

  • Christopher A. Reissaus

    (Indiana University School of Medicine)

  • Amelia K. Linnemann

    (Indiana University School of Medicine)

  • Elisa D’Este

    (Max Planck Institute for Medical Research)

  • Davide Calebiro

    (University of Birmingham
    Birmingham Health Partners)

  • Stefan Trapp

    (University College London)

  • Kai Johnsson

    (Max Planck Institute for Medical Research)

  • Tom Podewin

    (Max Planck Institute for Medical Research)

  • Johannes Broichhagen

    (Max Planck Institute for Medical Research)

  • David J. Hodson

    (University of Birmingham
    Birmingham Health Partners)

Abstract

The glucagon-like peptide-1 receptor (GLP1R) is a class B G protein-coupled receptor (GPCR) involved in metabolism. Presently, its visualization is limited to genetic manipulation, antibody detection or the use of probes that stimulate receptor activation. Herein, we present LUXendin645, a far-red fluorescent GLP1R antagonistic peptide label. LUXendin645 produces intense and specific membrane labeling throughout live and fixed tissue. GLP1R signaling can additionally be evoked when the receptor is allosterically modulated in the presence of LUXendin645. Using LUXendin645 and LUXendin651, we describe islet, brain and hESC-derived β-like cell GLP1R expression patterns, reveal higher-order GLP1R organization including membrane nanodomains, and track single receptor subpopulations. We furthermore show that the LUXendin backbone can be optimized for intravital two-photon imaging by installing a red fluorophore. Thus, our super-resolution compatible labeling probes allow visualization of endogenous GLP1R, and provide insight into class B GPCR distribution and dynamics both in vitro and in vivo.

Suggested Citation

  • Julia Ast & Anastasia Arvaniti & Nicholas H. F. Fine & Daniela Nasteska & Fiona B. Ashford & Zania Stamataki & Zsombor Koszegi & Andrea Bacon & Ben J. Jones & Maria A. Lucey & Shugo Sasaki & Daniel I., 2020. "Super-resolution microscopy compatible fluorescent probes reveal endogenous glucagon-like peptide-1 receptor distribution and dynamics," Nature Communications, Nature, vol. 11(1), pages 1-18, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14309-w
    DOI: 10.1038/s41467-020-14309-w
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