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

Ast, J., Arvaniti, A., Fine, N. H., Nasteska, D., Ashford, F. B., Stamataki, Z., et al. (2020). Super-resolution microscopy compatible fluorescent probes reveal endogenous glucagon-like peptide-1 receptor distribution and dynamics. Nature Communications, 11: 467 (2020), pp. 1-18. doi:10.1038/s41467-020-14309-w.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-9030-1 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-FE45-0
Genre: Journal Article

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 Creators:
Ast, Julia, Author
Arvaniti, Anastasia, Author
Fine, Nicholas H.F., Author
Nasteska, Daniela, Author
Ashford, Fiona B., Author
Stamataki, Zania, Author
Koszegi, Zsombor, Author
Bacon, Andrea, Author
Jones, Ben J., Author
Lucey, Maria A., Author
Sasaki, Shugo, Author
Brierley, Daniel I., Author
Hastoy, Benoit, Author
Tomas, Alejandra, Author
D’Agostino, Giuseppe, Author
Reimann, Frank, Author
Lynn, Francis C., Author
Reissaus, Christopher A., Author
Linnemann, Amelia K., Author
D´Este, Elisa1, Author              
Calebiro, Davide, AuthorTrapp, Stefan, AuthorJohnsson, Kai2, Author              Podewin, Tom3, Author              Broichhagen, Johannes2, Author              Hodson , David J., Author more..
Affiliations:
1Department of NanoBiophotonics, MPI for Biophysical Chemistry, Max Planck Society, ou_578627              
2Chemical Biology, Max Planck Institute for Medical Research, Max Planck Society, ou_2364732              
3Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              

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 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.

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Language(s): eng - English
 Dates: 2019-02-272019-12-272020-01-24
 Publication Status: Published online
 Pages: 18
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-020-14309-w
 Degree: -

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
 Creator(s):
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 11 Sequence Number: 467 (2020) Start / End Page: 1 - 18 Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723