Evidence map›Paper›PMID 39574659›Full record

ArticlebioRxiv : the preprint server for biology2024

The MRAP2 accessory protein directly interacts with melanocortin-3 receptor to enhance signaling.

Aqfan Jamaluddin, Rachael A Wyatt, Joon Lee, Georgina K C Dowsett, John A Tadross, Johannes Broichhagen, Giles S H Yeo, Joshua Levitz, Caroline M Gorvin

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Aqfan JamaluddinDepartment of Metabolism and Systems Science, University of Birmingham, Birmingham, UK.
Rachael A WyattDepartment of Metabolism and Systems Science, University of Birmingham, Birmingham, UK.
Joon LeeDepartment of Biochemistry, Weill Cornell Medicine, New York, NY 10065, USA.
Georgina K C DowsettWellcome-MRC Institute of Metabolic Science-Metabolic Research Laboratories, University of Cambridge, Cambridge, UK.
John A TadrossWellcome-MRC Institute of Metabolic Science-Metabolic Research Laboratories, University of Cambridge, Cambridge, UK.ORCID 0000-0002-8424-1252
Johannes BroichhagenLeibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), 13125, Berlin, Germany.ORCID 0000-0003-3084-6595
Giles S H YeoWellcome-MRC Institute of Metabolic Science-Metabolic Research Laboratories, University of Cambridge, Cambridge, UK.
Joshua LevitzDepartment of Biochemistry, Weill Cornell Medicine, New York, NY 10065, USA.
Caroline M GorvinDepartment of Metabolism and Systems Science, University of Birmingham, Birmingham, UK.ORCID 0000-0002-1361-9174

Funding

Mechanisms of Regulation of Metabotropic Glutamate ReceptorsR01NS129904 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI Joshua Levitz · 2023 to 2026
$2.6M
NINDS NIH HHS R01 NS129904Wellcome Trust
6 · The paper itself

Abstract

The central melanocortin system links nutrition to energy expenditure, with melanocortin-4 receptor (MC4R) controlling appetite and food intake, and MC3R regulating timing of sexual maturation, rate of linear growth and lean mass accumulation. Melanocortin-2 receptor accessory protein-2 (MRAP2) is a single transmembrane protein that interacts with MC4R to potentiate it's signalling, and human mutations in MRAP2 cause obesity. Previous studies have been unable to consistently show whether MRAP2 affects MC3R activity. Here we used single-molecule pull-down (SiMPull) to confirm that MC3R and MRAP2 interact in HEK293 cells. Analysis of fluorescent photobleaching steps showed that MC3R and MRAP2 readily form heterodimers most commonly with a 1:1 stoichiometry. Human single-nucleus and spatial transcriptomics show MRAP2 is co-expressed with MC3R in hypothalamic neurons with important roles in energy homeostasis and appetite control. Functional analyses showed MRAP2 enhances MC3R cAMP signalling, impairs β-arrestin recruitment, and reduces internalization in HEK293 cells. Structural homology models revealed putative interactions between the two proteins and alanine mutagenesis of five MRAP2 and three MC3R transmembrane residues significantly reduced MRAP2 effects on MC3R signalling. Finally, we showed genetic variants in MRAP2 that have been identified in individuals that are overweight or obese prevent MRAP2's enhancement of MC3R-driven signalling. Thus, these studies reveal MRAP2 as an important regulator of MC3R function and provide further evidence for the crucial role of MRAP2 in energy homeostasis.

Identifiers

PMID39574659
PMCPMC11580913

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