Real-time trafficking and signaling of the glucagon-like peptide-1 receptor

The Physiology of Glucagon-like Peptide 1

Holst, J. J. (2007) · Physiological Reviews · doi:10.1152/physrev.00034.2006 · Cited by 3,371

Pathways and mechanisms of endocytic recycling

Grant, B. D., & Donaldson, J. G. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2755 · Cited by 1,424

Molecular and Cellular Endocrinology

Rainey, W. E., & Rodgers, R. J. (2004) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2004.10.007 · Cited by 1,340

GLP-1 receptor agonists for individualized treatment of type 2 diabetes mellitus

Meier, J. J. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2012.140 · Cited by 1,311

Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV.

Kieffer, T. J., McIntosh, C. H., & Pederson, R. A. (1995) · Endocrinology · doi:10.1210/endo.136.8.7628397 · Cited by 1,124

Exendin-4 is a high potency agonist and truncated exendin-(9-39)-amide an antagonist at the glucagon-like peptide 1-(7-36)-amide receptor of insulin-secreting beta-cells.

Göke, R., Fehmann, H. C., Linn, T., Schmidt, H., Krause, M., Eng, J., & Göke, B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36565-2 · Cited by 837

Conformational biosensors reveal GPCR signalling from endosomes

Irannejad, R., Tomshine, J. C., Tomshine, J. R., Chevalier, M., Mahoney, J. P., Steyaert, J., Rasmussen, S. G. F., Sunahara, R. K., El-Samad, H., Huang, B., et al. (2013) · Nature · doi:10.1038/nature12000 · Cited by 819

Regulation of GPCRs by Endocytic Membrane Trafficking and Its Potential Implications

Hanyaloglu, A. C., & von Zastrow, M. (2007) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.48.113006.094830 · Cited by 610

International Union of Pharmacology. XXXV. The Glucagon Receptor Family

Mayo, K. E., Miller, L. J., BATAILLE, D., Dalle, S., Göke, B., Thorens, B., & Drucker, D. J. (2003) · Pharmacological Reviews · doi:10.1124/pr.55.1.6 · Cited by 514

Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: application to GPCR oligomerization

Maurel, D., Comps‐Agrar, L., Brock, C., Rives, M., Bourrier, E., Ayoub, M. A., Bazin, H., Tinel, N., Durroux, T., Prézeau, L., et al. (2008) · Nature Methods · doi:10.1038/nmeth.1213 · Cited by 500

Proinflammatory switch from Gαs to Gαi signaling by Glucagon-like peptide-1 receptor in murine splenic monocyte following burn injury

Zhang, Q., Hao, J.-W., Li, G., Ji, X.-J., Yao, X., Dong, N., & Yao, Y.-M. (2017) · Inflammation Research · doi:10.1007/s00011-017-1104-9 · Cited by 14

Evaluation of efficacy- versus affinity-driven agonism with biased GLP-1R ligands P5 and exendin-F1

Marzook, A., Chen, S., Pickford, P., Lucey, M., Wang, Y., Junior, I. R. C., Broichhagen, J., Hodson, D. J., Salem, V., Rutter, G. A., et al. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114656 · Cited by 14

LRRK2 exonic variants associated with Parkinson’s disease augment phosphorylation levels for LRRK2-Ser1292 and Rab10-Thr73Preprint

Christensen, K. V., Hentzer, M., Oppermann, F. S., Elschenbroich, S., Acheson-Dossang, P., Thirstrup, K., Egebjerg, J., Williamson, D. S., & Smith, G. P. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/447946 · Cited by 14

Pharmacological characterization of novel small molecule agonists and antagonists for the orphan receptor GPR139

Pallareti, L., Rath, T. F., Trapkov, B., Tsonkov, T. M., Nielsen, A. T., Harpsøe, K., Gentry, P. R., Bräuner‐Osborne, H., Gloriam, D. E. I., & Foster, S. R. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.175553 · Cited by 12

Positive Allosteric Modulators of Metabotropic Glutamate Receptor 5 as Tool Compounds to Study Signaling Bias

Arsova, A., Møller, T. C., Hellyer, S. D., Vedel, L., Foster, S. R., Hansen, J. L., Bräuner‐Osborne, H., & Gregory, K. J. (2021) · Molecular Pharmacology · doi:10.1124/molpharm.120.000185 · Cited by 13

Cardiovascular effects of GLP-1 receptor agonism

Winquist, R. J., & Gribkoff, V. K. (2022) · Advances in pharmacology · doi:10.1016/bs.apha.2022.02.005 · Cited by 14

GRK2 selectively attenuates the neutrophil NADPH-oxidase response triggered by β-arrestin recruiting GPR84 agonists

Fredríksson, J., Holdfeldt, A., Mårtensson, J., Björkman, L. I., Møller, T. C., Müllers, E., Dahlgren, C., Sundqvist, M., & Forsman, H. F. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119262 · Cited by 12

NanoSIMS Imaging Reveals the Impact of Ligand-ASO Conjugate Stability on ASO Subcellular Distribution

Kay, E. I., Stulz, R., Becquart, C., Lovrić, J., Tängemo, C., Thomen, A., Baždarević, D., Najafinobar, N., Dahlén, A., Pielach, A., et al. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14020463 · Cited by 12

Prolonged signaling of backbone-modified glucagon‐like peptide‐ 1 analogues with diverse receptor trafficking

Cary, B. P., Hager, M. V., Mariam, Z., Morris, R. K., Belousoff, M. J., Deganutti, G., Sexton, P. M., Wootten, D. L., & Gellman, S. H. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2407574122 · Cited by 12

GLP-1(28-36)amide, a Long Ignored Peptide Revisited

Huang, K., Zhou, B., Ji, K., Peng, A., & Yang, X. (2014) · The Open Biochemistry Journal · doi:10.2174/1874091x01408010107 · Cited by 11

Exploiting the Unique Properties of Lanthanide Complexes as FRET Probes: from Quantitation to Protein Dynamics

Wheeler, S., & Butler, S. J. (2022) · Analysis & Sensing · doi:10.1002/anse.202200036 · Cited by 13

Use of CRISPR/Cas9-edited HEK293 cells reveals that both conventional and novel protein kinase C isozymes are involved in mGlu5a receptor internalization

van Senten, J. R., Møller, T. C., Moo, E. V., Seiersen, S. D., & Bräuner‐Osborne, H. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102466 · Cited by 11

Endothelin-converting enzyme-1 regulates glucagon-like peptide-1 receptor signalling and resensitisation

Lu, J. N., & Willars, G. B. (2019) · Biochemical Journal · doi:10.1042/bcj20180853 · Cited by 11

Photo-SNAP-tag, a Light-Regulated Chemical Labeling System

Cleveland, J. D., & Tucker, C. L. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00412 · Cited by 12

Signaling Mechanism for Modulation by GLP-1 and Exendin-4 of GABA Receptors on Rat Retinal Ganglion Cells

Zhang, T., Ruan, H.-Z., Wang, Y., Shao, Y., Zhou, W., Weng, S.-J., & Zhong, Y. (2022) · Neuroscience Bulletin · doi:10.1007/s12264-022-00826-9 · Cited by 11

Associations between changes in glucagon‐like peptide‐1 and bodyweight reduction in patients receiving acarbose or metformin treatment

Wang, N., Zhang, J., Xing, X., Yang, Z., Zhang, B., Wang, X., & Yang, W. (2016) · Journal of Diabetes · doi:10.1111/1753-0407.12486 · Cited by 9

Rat cytomegalovirus-encoded γ-chemokine vXCL1 is a highly adapted, species-specific agonist for rat XCR1-positive dendritic cells

Bauer, A., Madela, J., Berg, C., Daugvilaite, V., Gurka, S., Mages, H. W., Kroczek, R. A., ROSENKILDE, M. M., & Voigt, S. (2019) · Journal of Cell Science · doi:10.1242/jcs.236190 · Cited by 10

Small-Molecule Ligands that Bind the RET Receptor Activate Neuroprotective Signals Independent of but Modulated by Coreceptor GFRα1

Jmaeff, S., Sidorova, Y. A., Lippiatt, H., Barcelona, P. F., Nedev, H. N., Saragovi, L. M., Hancock, M. A., Saarma, M., & Saragovi, H. U. (2020) · Molecular Pharmacology · doi:10.1124/mol.119.118950 · Cited by 10

GIP receptor: Expression in neuroendocrine tumours, internalization, signalling from endosomes and structure-function relationship studies

Reubi, J. C., Fourmy, D., Cordomí, A., Tikhonova, I. G., & Gigoux, V. (2019) · Peptides · doi:10.1016/j.peptides.2019.170229 · Cited by 10

Red and far-red cleavable fluorescent dyes for self-labelling enzyme protein tagging and interrogation of GPCR co-internalization

Roßmann, K., Birke, R., Levitz, J., Jones, B. J., & Broichhagen, J. (2024) · RSC Chemical Biology · doi:10.1039/d4cb00209a · Cited by 6

The role of mast cells in cellular modifications evoked by Exendin-4 in treated wounds: a preclinical study

Paroli, G., Murciano, N., Mancini, C., Soldaini, M. G. B., Rijli, S., DeSiena, G., & Bacci, S. (2022) · Journal of Wound Care · doi:10.12968/jowc.2022.31.8.701 · Cited by 6

Revolutionizing obesity treatment: The emerging role of GLP-1 receptor agonists and next-generation pharmacotherapies

Polu, P. R. (2026) · Obesity Medicine · doi:10.1016/j.obmed.2026.100686 · Cited by 5

A lipidated peptide derived from the C-terminal tail of the vasopressin 2 receptor shows promise as a new β-arrestin inhibitor

Brouillette, R. L., Mona, C. E., Desgagné, M., Hassanzedeh, M., Breault, É., Lussier, F., Belleville, K., Longpré, J., Grandbois, M., Boudreault, P., et al. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.107597 · Cited by 5

A Single Dose-Escalation Study to Evaluate the Safety and Pharmacokinetics of Orally Administered Des-Aspartate Angiotensin I in Healthy Subjects

Lee, K., Khoo, C.-M., Chowbay, B., Chan, Y., & Sim, M. (2016) · Drugs in R&D · doi:10.1007/s40268-016-0143-y · Cited by 5

Exploring the GLP-1–GLP-1R axis in porcine pancreas and gastrointestinal tract in vivo by ex vivo autoradiography

Manell, E., Puuvuori, E., Svensson, A. C., Velikyan, I., Hulsart‐Billström, G., Hedenqvist, P., Holst, J. J., Jensen‐Waern, M., & Eriksson, O. (2021) · BMJ Open Diabetes Research & Care · doi:10.1136/bmjdrc-2020-002083 · Cited by 5

Semaglutide drives weight loss through cAMP-dependent mechanisms in GLP1R-expressing hindbrain neurons

Gao, C., Geneve, I. C., Rodriguez-Gonzalez, S., Li, C., McElhern, K., Reitman, M. L., Lutas, A., & Krashes, M. J. (2026) · Nature Metabolism · doi:10.1038/s42255-026-01534-8 · Cited by 7

Reduced incretin receptor trafficking upon activation enhances glycemic control and reverses obesity in diet-induced obese mice

Bauri, R., Bele, S. D., Edelli, J., Reddy, N. C., Kurukuti, S., Devasia, T., Ibrahim, A., Rai, V., & Mitra, P. (2024) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00474.2023 · Cited by 3

The C-terminal regions of the GLP-1 and GIP receptors are not the key determinants of their differential arrestin recruitment but modulate the rate of receptor endocytosis

Al‐Zaid, B., & Al‐Sabah, S. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1528295 · Cited by 4

Fluorescent-Based Strategies to Investigate G Protein-Coupled Receptors: Evolution of the Techniques to a Better Understanding

Faklaris, O., Heuninck, J., Falco, A., Goyet, E., Zwier, J. M., Pin, J., Mouillac, B., Perroy, J., & Durroux, T. (2017) · Topics in medicinal chemistry · doi:10.1007/7355_2017_2 · Cited by 3

The impact of GLP-1 signalling on the energy metabolism of pancreatic islet β-cells and extrapancreatic tissues

Peart, L. A., Draper, M., & Tarasov, A. I. (2024) · Peptides · doi:10.1016/j.peptides.2024.171243 · Cited by 3

Building the Glucagon-Like Peptide-1 Receptor Brick by Brick: Revisiting a 1993 Diabetes Classic by Thorens et al.

Thorens, B., & Hodson, D. J. (2024) · Diabetes · doi:10.2337/dbi24-0025 · Cited by 3

Pharmacological characterization of a clinical candidate, TG-0054, a small molecule inverse agonist targeting CXCR4

Pan, K. S., Wang, Z., Pfeil, C., Bergkamp, N. D., Mobach, S., Roth, S., Rizk, A., Lohse, M. J., Annibale, P., Siderius, M. H., et al. (2025) · Molecular Pharmacology · doi:10.1016/j.molpha.2025.100015 · Cited by 2

Two-photon imaging of pancreatic beta cells in real time in vivo

Clardy, S. M., Köhler, R. H., Vinegoni, C., Iwamoto, Y., Keliher, E. J., & Weissleder, R. (2016) · TECHNOLOGY · doi:10.1142/s2339547816200028 · Cited by 2

Probing Self-Assembly of G Protein-Coupled Receptor Oligomers in Membranes Using Molecular Dynamics Modeling and Experimental Approaches

Sakmar, T. P., Périole, X., & Huber, T. (2017) · Springer eBooks · doi:10.1007/978-3-319-60174-8_15 · Cited by 2

Design, synthesis and characterization of a fluorescently labeled functional analog of full-length human ghrelin

Liu, M., Whitfield, E. A., Fothergill, L. J., Furness, J. B., Wade, J. D., Furness, S. G. B., & Hossain, M. A. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.09.028 · Cited by 2

Moderate preventative effect with intraperitoneal liraglutide injection in high-fat diet induced C57BL/6J obese mouse model

Khroud, M., Song, Z., Shao, W., & Jin, T. (2019) · Obesity Medicine · doi:10.1016/j.obmed.2019.100153 · Cited by 2

Systematic Characterisation of GLP ‐ 1R in Human Enteric Nervous System: Implications for GLP ‐1 as a Key Regulator of Colonic Activity

Dontamsetti, K. D., Aktar, R., & Peiris, M. (2026) · Journal of Neurochemistry · doi:10.1111/jnc.70461 · Cited by 1

Single-molecule labeling for studying trafficking of renal transporters

Jaykumar, A. B., Caceres, P. S., & Ortiz, P. A. (2018) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00082.2017 · Cited by 1

Comparative Analysis of a Series of pH‐Responsive Sulphonated Europium Complexes for Bioassays Monitoring Acidification

Fradgley, J. D., Starck, M., Lamarque, L., & Parker, D. (2022) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.202200426 · Cited by 2

GABA signaling regulation by GLP-1 receptor agonists and GABA-A receptors modulator

Babateen, O. (2016) · KTH Publication Database DiVA (KTH Royal Institute of Technology)

Molecular Imaging Agent Design for Quantifying Beta Cell Mass in Type 1 Diabetes

Zhang, L. (2017) · Deep Blue (University of Michigan)

G protein-Coupled Receptor Associated Sorting Protein GASP1 mediated trafficking of the Glucagon Like Peptide-1 Receptor contributes to the development of tolerance to incretin drugsPreprint

Gaur, A., Keeshen, C. M., King, M., Dirks, N., Flisher, M. F., Cummings, B. P., Huising, M. O., & Whistler, J. L. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.09.607397

Post-Inhibitory Rebound by δ-Cells Converts Inhibition into Excitation and Confers Islet PlasticityPreprint

Tamayo, A., Rodriguez, D. H., Pereira, E., Camacho-Becerra, S., Gonçalves, L. M., Bergreen, P.-O., Sokolov, M., Drigo, R. A. E., Alcazar, O., & Rodriguez‐Diaz, R. (2025) · SSRN Electronic Journal · doi:10.1101/2025.11.10.687745

NLRP3 activators disrupt the endocytic AP2 complex and plasma membrane signalingPreprint

Ebner, S., Phulphagar, K. M., Alvarez, Y., Jürgenliemke, L., Frechen, F., Stötzel, I., Lovotti, M., Mangan, M., Akbal, A., Schneberger, N., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.24.707400

Quercetin and lupeol accelerate keratinocyte wound healing by dual modulation of GLP-1 receptor activity and stability

Boonruang, K., Nilkhet, S., Kim, T. E., Krisanapun, C., Kim, S.-K., Ryu, J., & Baek, S. J. (2026) · Life Sciences · doi:10.1016/j.lfs.2026.124644

Analysis of CXCR4 and ACKR3 oligomerisation

Heuninck, J. (2019) · theses.fr (ABES) · doi:10.70675/e4fae036z07a1z4ab5z9730z70b3c09c88d4

Rôles des analogues du glucagon-like peptide 1 dans l’arthrose : caractérisation des effets analgésiques, anti-inflammatoires et structuraux du liraglutide

Meurot, C. (2022) · theses.fr (ABES) · doi:10.70675/a3a95a66z221ez48f8za375za47ba9766b15

Progressive loss of glycemic control during chronic DPP-4 inhibitor therapy despite preserved β-cell function: a case report suggesting acquired incretin resistance

Prasad, S., Ahuja, A., Sharma, S., Nagda, J., Agrawal, S., Parmar, V., & Vardhan, H. (2026) · Cardiovascular Diabetology – Endocrinology Reports · doi:10.1186/s40842-026-00296-2

GLP-1R and GIPR crosstalk modulates insulinotropic signaling pathways

Lindquist, P., Dijkhof, L. R. H., Drzazga, A. K., Sabatier, P., Stępniewski, T. M., Granlund, L., Lechner, M. Y., Zhong, Y., Gasbjerg, L. S., Hartmann, B., et al. (2026) · Cell chemical biology · doi:10.1016/j.chembiol.2026.06.003

A multi-scale quantitative systems pharmacology model of the Pharmaco-Nutritional Kinetic Paradox: GLP-1 receptor agonists, colonic fibre fermentation and endogenous GLP-1 signallingPreprint

Choudhary, A. K., & Sahu, S. (2026) · Research Square · doi:10.21203/rs.3.rs-10780569/v1

Molecular design and delivery of extracellular and membrane protein degradation chimeras

Lin, S., Zhou, H., Qiu, J., Dang, Y., Kou, L., Zhu, Z., Xu, Z., Lai, Y., & Yu, H. (2026) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2026.115959

The GLP-1–Gut Microbiota–Autoimmunity Axis in Type 1 Diabetes: Emerging Evidence and Mechanistic Perspectives

Arecco, A., Piras, G., Cocchiara, F., Maggi, D. C., & Puddu, A. (2026) · Diabetology · doi:10.3390/diabetology7100187

Landscape of Endocytic Effectors for Extracellular Targeted Protein Degradation

Liang, Y., Shao, S., Chen, Y., 司晶星, & Shen, Y. (2026) · Medicinal Research Reviews · doi:10.1002/med.70112

229-LB: Quantification of GLP-1R Internalization and Recycling in Live ß Cells

Gray, S. M., Sloop, K. W., Ravn, P., Campbell, J. E., & D’Alessio, D. A. (2021) · Diabetes · doi:10.2337/db21-229-lb

Functional Consequences of Glucagon-like Peptide-1 Receptor Cross-talk and Trafficking

Roed, S. N., Nøhr, A. C., Wismann, P., Iversen, H. K., Bräuner‐Osborne, H., Knudsen, S. M., & Waldhoer, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.592436 · Cited by 77

Ligand-Specific Factors Influencing GLP-1 Receptor Post-Endocytic Trafficking and Degradation in Pancreatic Beta Cells

Fang, Z., Chen, S., Manchanda, Y., Bitsi, S., Pickford, P., David, A., Shchepinova, M. M., Junior, I. R. C., Hodson, D. J., Broichhagen, J., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218404 · Cited by 44

The Interplay of Glucagon-Like Peptide-1 Receptor Trafficking and Signalling in Pancreatic Beta Cells

Marzook, A., Tomas, A., & Jones, B. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.678055 · Cited by 121

2114-P: Quantification of GLP-1R Trafficking in Primary Beta Cells in Response to Different Ligands

Gray, S. M., Ravn, P., Sloop, K. W., Campbell, J. E., & D’ALESSIO, J. (2020) · Diabetes · doi:10.2337/db20-2114-p