The ‘magic tail’ of G protein‐coupled receptors: an anchorage for functional protein networks

Bockaert, Joël; Marin, Philippe; Dumuis, Aline; Fagni, Laurent

doi:10.1016/s0014-5793(03)00453-8

Cited by 210 publications

(156 citation statements)

References 69 publications

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“…Interactions within such complexes can maintain the receptor at a specific location, alter its trafficking properties, or modulate function. The C-terminal tail of many GPCRs encompasses binding sites for interacting proteins, and this has resulted in this region being described as the "magic tail" of GPCRs (44) and "as an anchorage for functional protein networks" (44). A significant number of identified GPCR-interacting proteins also link to the actin cytoskeleton and thus may provide frameworks to define subcellular localization.…”

Section: Discussionmentioning

confidence: 99%

Periplakin Interferes with G Protein Activation by the Melanin-concentrating Hormone Receptor-1 by Binding to the Proximal Segment of the Receptor C-terminal Tail

Murdoch

Feng

Bächner

et al. 2005

Journal of Biological Chemistry

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The orexigenic cyclic 19 amino acid peptide melanin-concentrating hormone (MCH) 1 (1) is the natural ligand for the G protein-coupled receptor (GPCR) originally designated SLC-1 (also called GPR24 in some studies) because of its relatedness to the receptors for somatostatin (2-6). This polypeptide was thus renamed the MCH-1 receptor. A second MCH receptor (MCH-2 receptor) has also been identified (7-11), and there is some evidence of an MCH binding site that is distinct from these two receptors (12).Even before identification of the MCH receptors a clear role for MCH in feeding and energy balance and homeostasis had been established (1). A solid body of genetic and pharmacological evidence now supports a role for MCH and the MCH-1 receptor in the modulation of food intake and energy expenditure. Key data derive from the genetic ablation of both MCH (13) and the MCH-1 receptor (14, 15) in mice. These alterations produced animals that were both lean and resistant to dietinduced obesity. Mice lacking the MCH-1 receptor have been reported to be hyperphagic (14, 15) but to be both hyperactive and to have altered metabolism, and this may explain the apparent paradox of being resistant to obesity but eating more. Studies also indicate that acute and chronic administration of MCH enhances food intake and body weight (16) and that overexpression of MCH in transgenic mice leads to obesity and insulin resistance (17). A role for the MCH-2 receptor in these effects is unlikely because genetic evidence indicates that mice do not express a functional form of this receptor (18). Furthermore, the distribution of the MCH-1 receptor in the central nervous system (19) also suggests that antagonists at the MCH-1 receptor might provide a treatment for obesity (for review, see Refs. 20 and 21). High throughput screening efforts have led to the identification of small molecule MCH-1 receptor antagonists with diverse structural features and drug-like properties. In vivo results with two of these antagonists indicate efficacy in several animal models of body weight regulation and feeding behavior (21). At least when expressed in

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Section: Discussionmentioning

confidence: 99%

Periplakin Interferes with G Protein Activation by the Melanin-concentrating Hormone Receptor-1 by Binding to the Proximal Segment of the Receptor C-terminal Tail

Murdoch

Feng

Bächner

et al. 2005

Journal of Biological Chemistry

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“…In 2003, already 50 or more GIPs had been demonstrated and Bockaert et al (2003Bockaert et al ( , 2010 in an interesting review described the C-terminal tail of the GPCRs as the 'magic tail' representing an important anchorage for functional protein networks. Thus, receptor complexes are in the center of multiple receptor-protein and protein-protein interactions that can influence their assemblage and stoichiometry (see Fuxe et al, 2014b).…”

Section: Gpcr Interacting Proteins (Gips)mentioning

confidence: 99%

G protein-coupled receptor-receptor interactions give integrative dynamics to intercellular communication

Guidolin

Marcoli

Tortorella

et al. 2018

Reviews in the Neurosciences

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Abstract:The proposal of receptor-receptor interactions (RRIs) in the early 1980s broadened the view on the role of G protein-coupled receptors (GPCR) in the dynamics of the intercellular communication. RRIs, indeed, allow GPCR to operate not only as monomers but also as receptor complexes, in which the integration of the incoming signals depends on the number, spatial arrangement, and order of activation of the protomers forming the complex. The main biochemical mechanisms controlling the functional interplay of GPCR in the receptor complexes are direct allosteric interactions between protomer domains. The formation of these macromolecular assemblies has several physiologic implications in terms of the modulation of the signaling pathways and interaction with other membrane proteins. It also impacts on the emerging field of connectomics, as it contributes to set and tune the synaptic strength. Furthermore, recent evidence suggests that the transfer of GPCR and GPCR complexes between cells via the exosome pathway could enable the target cells to recognize/decode transmitters and/or modulators for which they did not express the pertinent receptors. Thus, this process may also open the possibility of a new type of redeployment of neural circuits. The fundamental aspects of GPCR complex formation and function are the focus of the present review article.

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“…involved in trafficking, and scaffolds that link the receptor to the elements of other signalling pathways (Brady and Limbird 2002;Hall and Lefkowitz 2002;Bockaert et al 2003). G proteins that couple to the M 2 muscarinic receptor are absent from Sf9 cells (Heitz et al 1995;Parker et al 1991); similarly, at least some chaperones are absent altogether or scarce relative to the levels of protein obtained upon baculoviral infection (Higgins et al 2003).…”

Section: Oligomers Of the M 2 Muscarinic Receptor 543mentioning

confidence: 99%

Oligomeric potential of the M₂ muscarinic cholinergic receptor

Park

Wells

2004

Journal of Neurochemistry

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G protein-coupled receptors are known to exist as oligomers. Although such aggregates often are referred to as dimers, there is little direct evidence regarding their oligomeric size. In the present investigation, c-Myc-, FLAG-, and influenza hemagglutinin (HA)-tagged forms of the M 2 muscarinic receptor have been coexpressed in Sf9 cells to probe for aggregates larger than a dimer. Immunochromatography, immunoprecipitation, and immunoblotting were carried out with various combinations of antibodies directed against the different epitopes to demonstrate that all three tagged forms of the receptor can be immunopurified within a single complex. Extracts of the M 2 muscarinic receptor from Sf9 cells therefore contain aggregates that are at least trimeric, and the levels detected point to the existence of larger complexes. The data also suggest that the oligomers coexist with a sizeable population of monomers.

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The ‘magic tail’ of G protein‐coupled receptors: an anchorage for functional protein networks

Cited by 210 publications

References 69 publications

Periplakin Interferes with G Protein Activation by the Melanin-concentrating Hormone Receptor-1 by Binding to the Proximal Segment of the Receptor C-terminal Tail

Periplakin Interferes with G Protein Activation by the Melanin-concentrating Hormone Receptor-1 by Binding to the Proximal Segment of the Receptor C-terminal Tail

G protein-coupled receptor-receptor interactions give integrative dynamics to intercellular communication

Oligomeric potential of the M₂ muscarinic cholinergic receptor

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The ‘magic tail’ of G protein‐coupled receptors: an anchorage for functional protein networks

Cited by 210 publications

References 69 publications

Periplakin Interferes with G Protein Activation by the Melanin-concentrating Hormone Receptor-1 by Binding to the Proximal Segment of the Receptor C-terminal Tail

Periplakin Interferes with G Protein Activation by the Melanin-concentrating Hormone Receptor-1 by Binding to the Proximal Segment of the Receptor C-terminal Tail

G protein-coupled receptor-receptor interactions give integrative dynamics to intercellular communication

Oligomeric potential of the M2 muscarinic cholinergic receptor

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Oligomeric potential of the M₂ muscarinic cholinergic receptor