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

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. Brierley, Benoit Hastoy, Alejandra Tomas, Giuseppe D’Agostino, Frank Reimann, Francis C. Lynn, Christopher A. Reissaus, Amelia K. Linnemann, Elisa D’Este, Davide Calebiro, Stefan Trapp, Kai Johnsson, Tom Podewin (), Johannes Broichhagen () and David J. Hodson ()
Additional contact information
Julia Ast: University of Birmingham
Anastasia Arvaniti: University of Birmingham
Nicholas H. F. Fine: University of Birmingham
Daniela Nasteska: University of Birmingham
Fiona B. Ashford: University of Birmingham
Zania Stamataki: University of Birmingham
Zsombor Koszegi: University of Birmingham
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
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

Nature Communications, 2020, vol. 11, issue 1, 1-18

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-14309-w

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