ÉR

Éric Reiter

Physiologie de la Reproduction et des Comportements

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Co-Authors

Pascale Crépieux

Physiologie de la Reproduction et des Comportements

Anne Poupon

Centre National de la Recherche Scientifique

Thomas Bourquard

Physiologie de la Reproduction et des Comportements

Florian Guillou

Physiologie de la Reproduction et des Comportements

Astrid Musnier

Physiologie de la Reproduction et des Comportements

Thomas Boulo

Physiologie de la Reproduction et des Comportements

Christophe Gauthier

Laboratoire Interdisciplinaire des Environnements Continentaux

Mohammed Akli Ayoub

Khalifa University of Science and Technology

Nathalie Gallay

Université de Tours

Romain Yvinec

Physiologie de la Reproduction et des Comportements

Cooperative Institutions

Centre National de la Recherche Scientifique

205

Howard Hughes Medical Institute

113

Université de Tours

108

Inserm

105

Physiologie de la Reproduction et des Comportements

104

Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement

National Institutes of Health

Harvard University

University of California, San Diego

Duke Medical Center

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GH and Growth Factors in Endocrinology and Metabolism - 36th International Symposium

Albert Beckers P Czernichow Éric Reiter M. L. Vance

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A single domain intrabody targeting the follicle-stimulating hormone receptor (FSHR) impacts FSH-induced G protein-dependent signalling

bioRxiv (Cold Spring Harbor Laboratory) (2023)

Pauline Raynaud Vinesh Jugnarain Océane Vaugrente Amandine Vallet Thomas Boulo

Abstract Intracellular variable fragments from heavy-chain antibody from camelids (intra-VHH) have been successfully used as chaperones to solve the 3D structure of active G protein-coupled receptors bound to their transducers. However, their effect on signalling has been poorly explored, although they may provide a better understanding on the relationships between receptor conformation and activity. Here, we isolated and characterized iPRC1, the first intra-VHH recognizing a member of the large glycoprotein hormone receptors family, the follicle-stimulating hormone receptor (FSHR). This intra-VHH recognizes the FSHR 3 rd intracellular loop and decreases cAMP production in response to FSH, without altering Gαs recruitment. Hence, iPRC1 behaves as an allosteric modulator and provides a new tool to complete structure/activity studies performed so far on this receptor.

Follicle-stimulating hormone receptor

10.1101/2023.08.07.552286

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Citations (1)

Unraveling the molecular architecture of a G protein-coupled receptor/β-arrestin/Erk module complex

Scientific Reports (2015)

Thomas Bourquard Flavie Landomiel Éric Reiter Pascale Crépieux David W. Ritchie

Abstract β-arrestins serve as signaling scaffolds downstream of G protein-coupled receptors and thus play a crucial role in a plethora of cellular processes. Although it is largely accepted that the ability of β-arrestins to interact simultaneously with many protein partners is key in G protein-independent signaling of GPCRs, only the precise knowledge of these multimeric arrangements will allow a full understanding of the dynamics of these interactions and their functional consequences. However, current experimental procedures for the determination of the three-dimensional structures of protein-protein complexes are not well adapted to analyze these short-lived, multi-component assemblies. We propose a model of the receptor/β-arrestin/Erk1 signaling module, which is consistent with most of the available experimental data. Moreover, for the β-arrestin/Raf1 and the β-arrestin/ERK interactions, we have used the model to design interfering peptides and shown that they compete with both partners, hereby demonstrating the validity of the predicted interaction regions.

Arrestin

Component (thermodynamics)

10.1038/srep10760

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Citations (49)

A single domain intrabody as a novel tool to bias the subcellular trafficking of the follicle-stimulating hormone receptor

bioRxiv (Cold Spring Harbor Laboratory) (2025)

Pauline Raynaud J Gourdon Vinesh Jugnarain L. Berthet Frédéric Jean‐Alphonse

Intracellular variable fragments from heavy-chain only antibodies of camelids (intra-VHH) have been successfully used for their stabilizing properties to solve the 3D structure of active G protein-coupled receptors (GPCRs) bound to their cognate transducers. They also provide tools to link a given conformation of a GPCR to the signalling network engaged, thus allowing extensive structure/activity studies. Recently, they have been instrumental in tracking active GPCRs in various subcellular compartments. Here, we report the isolation and characterization of iPRC2, an intra-VHH recognizing the 1st and 3rd intracellular loops of the FSHR, but not of the luteinizing hormone/choriogonadotropin receptor close relative. Its expression in the cell decreases the cAMP production in response to hormone binding, and requires G𝛼s for optimal interaction with the receptor. Importantly, iPRC2 increases the FSHR accumulation in the early endosomes, and consequently, diminishes its recycling to the cell surface. Hence, in contrast to previously described intra-VHH that disclose active GPCR intracellular location, iPRC2 provokes per se a location bias, through its ability to reroute the FSHR. Thus, it is an innovative tool to examine the functional consequences of GPCR accumulation in various sub-cellular compartments.

Follicle-stimulating hormone receptor

10.1101/2025.02.13.638052

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Molecular Mechanism of β-Arrestin-Biased Agonism at Seven-Transmembrane Receptors

The Annual Review of Pharmacology and Toxicology (2011)

Éric Reiter Seungkirl Ahn Arun K. Shukla R.J. Lefkowitz

The concept of biased agonism has recently come to the fore with the realization that seven-transmembrane receptors (7TMRs, also known as G protein–coupled receptors, or GPCRs) activate complex signaling networks and can adopt multiple active conformations upon agonist binding. As a consequence, the “efficacy” of receptors, which was classically considered linear, is now recognized as pluridimensional. Biased agonists selectively stabilize only a subset of receptor conformations induced by the natural “unbiased” ligand, thus preferentially activating certain signaling mechanisms. Such agonists thus reveal the intriguing possibility that one can direct cellular signaling with unprecedented precision and specificity and support the notion that biased agonists may identify new classes of therapeutic agents that have fewer side effects. This review focuses on one particular class of biased ligands that has the ability to alter the balance between G protein–dependent and β-arrestin-dependent signal transduction.

Functional selectivity

Arrestin

Agonism

Rhodopsin-like receptors

10.1146/annurev.pharmtox.010909.105800

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Citations (545)

mRNA-Selective Translation Induced by FSH in Primary Sertoli Cells

Molecular Endocrinology (2012)

Astrid Musnier Kelly E. Leon Julia Morales Éric Reiter Thomas Boulo

Abstract FSH is a key hormonal regulator of Sertoli cell secretory activity, required to optimize sperm production. To fulfil its biological function, FSH binds a G protein-coupled receptor, the FSH-R. The FSH-R-transduced signaling network ultimately leads to the transcription or down-regulation of numerous genes. In addition, recent evidence has suggested that FSH might also regulate protein translation. However, this point has never been demonstrated conclusively yet. Here we have addressed this issue in primary rat Sertoli cells endogenously expressing physiological levels of FSH-R. We observed that, within 90 min of stimulation, FSH not only enhanced overall protein synthesis in a mammalian target of rapamycin-dependent manner but also increased the recruitment of mRNA to polysomes. m7GTP pull-down experiments revealed the functional recruitment of mammalian target of rapamycin and p70 S6 kinase to the 5′cap, further supported by the enhanced phosphorylation of one of p70 S6 kinase targets, the eukaryotic initiation factor 4B. Importantly, the scaffolding eukaryotic initiation factor 4G was also recruited, whereas eukaryotic initiation factor 4E-binding protein, the eukaryotic initiation factor 4E generic inhibitor, appeared to play a minor role in translational regulations induced by FSH, in contrast to what is generally observed in response to anabolic factors. This particular regulation of the translational machinery by FSH stimulation might support mRNA-selective translation, as shown here by quantitative RT-PCR amplification of the c-fos and vascular endothelial growth factor mRNA but not of all FSH target mRNA, in polysomal fractions. These findings add a new level of complexity to FSH biological roles in its natural target cells, which has been underappreciated so far.

Translational regulation

Eukaryotic initiation factor

Maturation promoting factor

EIF4E

10.1210/me.2011-1267

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Citations (32)

Contributors

Elsevier eBooks (2021)

Ana Aranda Denise D. Belsham Véronique Bozon Maria Luisa Brandi Giulia Brigante

10.1016/b978-0-12-819801-8.09992-0

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Cellular Adhesion of Primary Sertoli Cells Affects Responsiveness of the Extracellular Signal-Regulated Kinases 1 and 2 to Follicle-Stimulating Hormone but Not to Epidermal Growth Factor

Archives of Biochemistry and Biophysics (2002)

Pascale Crépieux Nadine Martinat Sébastien Marion Florian Guillou Éric Reiter

10.1006/abbi.2002.2773

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Citations (23)

FSH-stimulated PTEN activity accounts for the lack of FSH mitogenic effect in prepubertal rat Sertoli cells

Molecular and Cellular Endocrinology (2009)

Joëlle Dupont Astrid Musnier Jérémy Decourtye Thomas Boulo Charlotte Lécureuil

Tensin

Follicle-stimulating hormone receptor

Phosphoinositide 3-kinase

10.1016/j.mce.2009.09.016

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Citations (36)

Bioluminescence Resonance Energy Transfer as a Method to Study Protein-Protein Interactions: Application to G Protein Coupled Receptor Biology

Molecules (2019)

Chayma El Khamlichi Flora Reverchon Nadège Hervouet‐Coste L. Blot Éric Reiter

The bioluminescence resonance energy transfer (BRET) approach involves resonance energy transfer between a light-emitting enzyme and fluorescent acceptors. The major advantage of this technique over biochemical methods is that protein-protein interactions (PPI) can be monitored without disrupting the natural environment, frequently altered by detergents and membrane preparations. Thus, it is considered as one of the most versatile technique for studying molecular interactions in living cells at “physiological” expression levels. BRET analysis has been applied to study many transmembrane receptor classes including G-protein coupled receptors (GPCR). It is well established that these receptors may function as dimeric/oligomeric forms and interact with multiple effectors to transduce the signal. Therefore, they are considered as attractive targets to identify PPI modulators. In this review, we present an overview of the different BRET systems developed up to now and their relevance to identify inhibitors/modulators of protein–protein interaction. Then, we introduce the different classes of agents that have been recently developed to target PPI, and provide some examples illustrating the use of BRET-based assays to identify and characterize innovative PPI modulators in the field of GPCRs biology. Finally, we discuss the main advantages and the limits of BRET approach to characterize PPI modulators.

10.3390/molecules24030537

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Citations (46)