Affinage

MRAP2

Melanocortin-2 receptor accessory protein 2 · UniProt Q96G30

Length
205 aa
Mass
23.5 kDa
Annotated
2026-04-28
51 papers in source corpus 18 papers cited in narrative 18 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

MRAP2 is a single-pass transmembrane accessory protein that functions as a broad-spectrum modulator of G protein-coupled receptor signaling, trafficking, and oligomerization, with a central role in energy homeostasis. MRAP2 forms antiparallel homodimers and engages multiple GPCRs — including MC2R, MC3R, MC4R, GHSR1a, OX1R, PKR1/PKR2, MCHR1, and melatonin receptors — predominantly as 1:1 complexes that disrupt receptor homodimerization; it enhances G protein-mediated signaling (Gs-cAMP, Gαq) while suppressing β-arrestin recruitment by blocking GRK2/PKC-mediated receptor phosphorylation, with distinct MRAP2 domains governing these biased signaling outputs (PMID:31911434, PMID:35605660, PMID:41722048, PMID:41401256). In neurons, MRAP2 is required for MC4R targeting to primary cilia and potentiates hypothalamic MC4R signaling to control food intake and energy expenditure; in pancreatic δ cells it enables ghrelin-GHSR1a signaling to regulate insulin secretion (PMID:36692018, PMID:30352741, PMID:32535024). Loss-of-function MRAP2 variants are associated with human obesity and disrupt signaling enhancement across multiple receptor partners, with structural models identifying shared transmembrane contact sites on MC4R helices 5 and 6 as critical interaction interfaces (PMID:39807633, PMID:36077245, PMID:40998819).

Mechanistic history

Synthesis pass · year-by-year structured walk · 9 steps
  1. 2009 High

    The question of whether MRAP2 regulates receptors beyond MC2R was answered: MRAP2 interacts with all five melanocortin receptors and bidirectionally modulates their signaling, establishing it as a general MCR accessory protein rather than an MC2R-specific chaperone.

    Evidence Co-immunoprecipitation, surface expression, and cAMP assays across MC1R–MC5R in heterologous cells

    PMID:19329486

    Open questions at the time
    • Mechanism of differential regulation (facilitation of MC2R vs. inhibition of MC1R/MC3R–MC5R) was not resolved
    • In vivo relevance in mammalian physiology not yet established
    • Stoichiometry and topology of MRAP2–MCR complexes unknown
  2. 2013 High

    Whether MRAP2 has developmental physiological functions in vivo was resolved: zebrafish MRAP2 isoforms differentially tune MC4R ligand sensitivity to control growth during distinct developmental stages, providing the first in vivo demonstration that MRAP2 is a physiological regulator of energy balance.

    Evidence Zebrafish genetic models with binding/signaling assays and in vivo growth phenotyping

    PMID:23869017

    Open questions at the time
    • Whether mammalian MRAP2 similarly controls MC4R in a developmental manner was not tested
    • Molecular basis for isoform-specific modulation of ligand affinity unknown
  3. 2017 High

    The scope of MRAP2 as a GPCR modulator was expanded beyond melanocortin receptors: MRAP2 interacts with and potentiates ghrelin receptor (GHSR1a) signaling in vitro and in vivo, while inhibiting OX1R and PKR1, demonstrating that MRAP2 is a multi-GPCR regulatory hub with receptor-specific outcomes.

    Evidence Co-IP and signaling assays for GHSR1a, OX1R, and PKR1; MRAP2 KO mice with neuronal activation phenotyping

    PMID:28939058 PMID:28959025

    Open questions at the time
    • Structural basis for receptor-specific facilitation vs. inhibition unknown
    • Whether MRAP2 regulates GHSR1a and OX1R/PKR1 simultaneously in the same cell not addressed
  4. 2018 High

    The circuit-level question of where MRAP2 acts in the brain to control energy balance was addressed: overexpression of MRAP2 specifically in PVN MC4R neurons reduces food intake and increases energy expenditure, establishing the hypothalamic paraventricular nucleus as a key site of MRAP2 action.

    Evidence Stereotaxic AAV-mediated MRAP2 overexpression in Mc4r-Cre mice with metabolic and c-Fos phenotyping

    PMID:30352741

    Open questions at the time
    • Contribution of other hypothalamic nuclei or peripheral tissues not dissected
    • Whether endogenous MRAP2 expression levels are rate-limiting in the PVN not determined
  5. 2020 High

    How MRAP2 achieves signaling bias was clarified: MRAP2 uses distinct domains to enhance Gαq-coupled signaling while blocking β-arrestin recruitment to GHSR1a, and separately requires MRAP2 in pancreatic δ cells for ghrelin-dependent insulin regulation, revealing both the molecular logic of biased signaling and a peripheral metabolic function.

    Evidence Domain-mapping mutagenesis with Gαq/β-arrestin assays; conditional δ-cell MRAP2 KO mice with calcium imaging and insulin secretion assays

    PMID:31911434 PMID:32535024

    Open questions at the time
    • Specific MRAP2 residues mediating domain-selective effects on bias not identified
    • Whether β-arrestin suppression operates by the same mechanism across all GPCR partners not tested
  6. 2021 Medium

    The topology question — how MRAP2 dimers are arranged in the membrane — was resolved: MRAP2 forms symmetric antiparallel homodimers, and orientation of individual domains within the dimer is functionally important for MC4R regulation.

    Evidence Chimeric domain-inversion constructs with surface expression and cAMP assays

    PMID:34759891

    Open questions at the time
    • Whether antiparallel dimer persists in the MRAP2–GPCR complex or dissociates upon receptor binding not determined
    • No high-resolution structural data confirming the dimer interface
  7. 2022 High

    The mechanism by which MRAP2 suppresses β-arrestin recruitment was identified: MRAP2 blocks GRK2 and PKC from phosphorylating GHSR1a at Ser252/Thr261 in the third intracellular loop, and separately MRAP2 interactions extend to MCHR1 and PKR2, broadening the receptor repertoire further.

    Evidence Phosphorylation-site mutagenesis and kinase interaction assays for GHSR1a; Co-IP/BiFC for MCHR1 and PKR2; obesity-linked R125H/R125C mutagenesis for PKR2

    PMID:35311242 PMID:35605660 PMID:36077245 PMID:38392222

    Open questions at the time
    • Whether GRK2/PKC blockade is the universal mechanism for β-arrestin suppression at all MRAP2-regulated GPCRs not established
    • Structural basis for how MRAP2 sterically occludes kinase access unknown
  8. 2023 High

    A subcellular targeting function was discovered: MRAP2 is required for MC4R localization to primary cilia in neurons, and this ciliary targeting is essential for MC4R-dependent weight regulation, revealing a trafficking role beyond plasma membrane delivery.

    Evidence Conditional MRAP2 KO in MC4R neurons, ciliary immunofluorescence, body weight and feeding phenotyping

    PMID:36692018

    Open questions at the time
    • Molecular mechanism of ciliary targeting (adaptor interactions, IFT involvement) not identified
    • Whether MRAP2 escorts other GPCRs to cilia not tested
  9. 2025 High

    A unifying structural and mechanistic framework emerged: MRAP2 engages MC4R, MC3R, and GHSR1a as 1:1 complexes via shared transmembrane contacts (MC4R TM5/6), disrupts GPCR homodimerization, and uses its C-terminal cytoplasmic domain to modulate constitutive activity; obesity-associated MRAP2 variants disrupt these conserved mechanisms across all tested receptors, and the receptor repertoire extends further to melatonin receptors.

    Evidence Single-molecule pull-down stoichiometry, FRET-based oligomerization, transmembrane alanine mutagenesis, multi-pathway signaling assays (cAMP, IP3, β-arrestin), structural homology modeling across MC4R/MC3R/GHSR1a; Co-IP/BiFC for melatonin receptors

    PMID:39807633 PMID:40510472 PMID:40998819 PMID:41401256 PMID:41722048

    Open questions at the time
    • No experimental high-resolution structure of an MRAP2–GPCR complex exists
    • How MRAP2 achieves receptor-specific outcomes (enhancement vs. inhibition) through shared contact sites remains unresolved
    • In vivo validation of transmembrane contact-site mutations not performed

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include: the high-resolution structure of MRAP2–GPCR complexes, the molecular determinants that dictate whether MRAP2 enhances or inhibits a given receptor, whether MRAP2 simultaneously regulates multiple GPCRs in the same neuron, and how ciliary targeting is mechanistically achieved.
  • No cryo-EM or crystal structure of any MRAP2–GPCR complex
  • Rules governing receptor-specific enhancement vs. inhibition not defined
  • Simultaneous multi-GPCR regulation in single cells not addressed

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 7 GO:0060090 molecular adaptor activity 3
Localization
GO:0005886 plasma membrane 3 GO:0005929 cilium 1
Pathway
R-HSA-162582 Signal Transduction 7 R-HSA-392499 Metabolism of proteins 3 R-HSA-1643685 Disease 2
Partners
GHSRMC2RMC3RMC4RMCHR1OX1RPROKR1PROKR2
Complex memberships
MRAP2 antiparallel homodimer

Evidence

Reading pass · 18 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2009 MRAP2 interacts with all five melanocortin receptors (MC1R–MC5R). This interaction enables MC2R surface expression and signaling, while reducing MC1R, MC3R, MC4R, and MC5R responsiveness to NDP-MSH — establishing MRAP2 as a bidirectional regulator of the MCR family. Co-immunoprecipitation, cell surface expression assays, cAMP signaling assays in heterologous cells Proceedings of the National Academy of Sciences of the United States of America High 19329486
2013 In zebrafish, MRAP2a binds MC4R and reduces ligand binding affinity for α-MSH, thereby blocking MC4R activity and stimulating growth during larval development, while MRAP2b also binds MC4R but increases ligand sensitivity, enhancing responsiveness to α-MSH once feeding begins — demonstrating developmental control of MC4R by MRAP2 isoforms. Zebrafish genetic model, cell culture binding and signaling assays, in vivo growth phenotyping Science High 23869017
2017 MRAP2 interacts with the ghrelin receptor GHSR1a and potentiates ghrelin-stimulated G protein signaling both in vitro and in vivo. In MRAP2-deficient mice, fasting fails to activate AgRP neurons and the orexigenic effect of ghrelin is lost. Co-immunoprecipitation (MRAP2–GHSR1a interaction), in vitro cAMP/signaling assays, MRAP2 knockout mouse model with neuronal activation readout Nature communications High 28959025
2017 MRAP2 interacts with and inhibits the trafficking and signaling of orexin receptor 1 (OX1R) and prokineticin receptor 1 (PKR1). Specific regions of MRAP2 are required for regulation of OX1R and PKR1. Co-immunoprecipitation, cell surface trafficking assays, domain-mapping experiments with MRAP2 truncation mutants Biochimica et biophysica acta. Molecular cell research Medium 28939058
2020 MRAP2 inhibits the constitutive activity of GHSR1a, enhances G protein-dependent (Gαq) signaling in response to ghrelin, and blocks β-arrestin recruitment and signaling. The effects on Gαq and β-arrestin pathways involve distinct regions of MRAP2, establishing biased signaling modulation by an accessory protein. Gαq and β-arrestin signaling assays, domain-mapping of MRAP2, constitutive activity assays in heterologous cells Science signaling High 31911434
2020 MRAP2 is expressed in pancreatic islet δ cells and is required for ghrelin to elicit a calcium response in those cells. Global and δ-cell-targeted deletion of MRAP2 abrogates the insulinostatic effect of ghrelin, establishing MRAP2 as a regulator of insulin secretion via δ-cell GHSR1a signaling. Calcium imaging in δ cells, global and conditional (δ cell-specific) MRAP2 knockout mouse models, insulin secretion assays iScience High 32535024
2022 MRAP2 inhibits β-arrestin recruitment to GHSR1a by blocking GRK2 and PKC from phosphorylating the receptor at Ser252 and Thr261 in the third intracellular loop. The C-terminal tail of GHSR1a is not essential for β-arrestin interaction. Phosphorylation site mutagenesis, GRK2/PKC interaction assays, β-arrestin recruitment assays The Journal of biological chemistry High 35605660
2022 Arginine 125 in MRAP2 is essential for protein conformation, dimer formation, and PKR2 binding. Human obesity-associated mutations R125H and R125C disrupt these functions. MRAP2 mutant characterization (R125H, R125C), dimerization assays, PKR2 co-immunoprecipitation, comparison with mouse MRAP2 International journal of molecular sciences Medium 36077245
2022 MRAP2 interacts with melanin-concentrating hormone receptor 1 (MCHR1) as shown by co-immunoprecipitation and bimolecular fluorescence complementation, and inhibits MCHR1 signaling. The C-terminal domain of MRAP2 is required for pharmacological modulation of intracellular Ca2+ cascades and membrane transport of MCHR1. Co-immunoprecipitation, BiFC assay, functional truncation mapping, intracellular Ca2+ signaling assay Frontiers in endocrinology Medium 35311242
2023 MRAP2 is critical for the ciliary localization of MC4R in neurons. Loss of MRAP2 disrupts MC4R targeting to the primary cilium, and this ciliary localization is essential for the weight-regulating function of MC4R neurons and long-term energy homeostasis. Conditional mouse models (MRAP2 KO in MC4R neurons), live imaging/immunofluorescence of primary cilia localization, body weight and food intake phenotyping JCI insight High 36692018
2024 MRAP2 inhibits β-arrestin-2 recruitment to prokineticin receptor 2 (PKR2) without preventing receptor internalization, modulating PKR2-mediated β-arrestin signaling pathways. β-arrestin recruitment assays, receptor internalization assays, signaling pathway analysis Current issues in molecular biology Medium 38392222
2025 MRAP2 co-expression increases MC4R G protein-mediated signaling, impairs β-arrestin2 recruitment and receptor internalization, and disrupts MC4R oligomers, increasing the proportion of monomeric MC4R. A structural homology model identifies MRAP2 interaction sites relevant for receptor activation. cAMP signaling assays, β-arrestin2 recruitment assays, FRET/fluorescence-based oligomerization assays, structural homology modeling Nature communications High 40998819
2025 MRAP2 directly interacts with MC3R with 1:1 stoichiometry, enhances MC3R cAMP signaling, impairs β-arrestin recruitment, and reduces MC3R internalization. Alanine mutagenesis of five MRAP2 and three MC3R transmembrane residues identified by structural homology modeling disrupts these effects. Obesity-associated MRAP2 variants fail to enhance MC3R signaling. Single-molecule pull-down (SiMPull), fluorescence photobleaching stoichiometry, cAMP assay, β-arrestin recruitment assay, internalization assay, transmembrane alanine mutagenesis, structural homology modeling Science signaling High 41401256
2025 MRAP2 interacts with MC4R, MC3R, and GHSR1a preferentially as 1:1 complexes (disrupting GPCR homodimerization), using shared receptor transmembrane region contacts to promote G protein signaling and impair β-arrestin-2 recruitment. Deletion of the MRAP2 cytoplasmic C-terminal region impairs GPCR signaling by modulating receptor constitutive activity. Obesity-associated MRAP2 variants modify constitutive activity of all three GPCRs. Single-molecule pull-down stoichiometry, GPCR homodimerization assays, domain deletion mutagenesis, constitutive activity assays, β-arrestin-2 recruitment assays for three receptors Cell reports High 41722048
2025 Obesity-associated MRAP2 variants impair multiple MC4R signaling pathways including Gs-cAMP and Gq-IP3; seven variants impair cAMP signaling and nine impair IP3 signaling. Four mutations in the MRAP2 C-terminus affect MC4R internalization. Structural models predict MRAP2 interacts with MC4R transmembrane helices 5 and 6, and mutagenesis of these contact sites impairs MRAP2-facilitated MC4R signaling. cAMP signaling assay, IP3 signaling assay, internalization assay, cell surface expression assay, structural homology modeling, contact-site alanine mutagenesis Human molecular genetics High 39807633
2018 Overexpression of MRAP2 specifically in PVN MC4R-expressing neurons reduces food intake, increases energy expenditure, and enhances neuronal activation at baseline and after MC3R/MC4R agonist treatment, demonstrating a site-specific role for MRAP2 in potentiating MC4R signaling in the hypothalamic paraventricular nucleus. Stereotaxic AAV-mediated MRAP2 overexpression in Mc4r-cre mice (PVN-targeted), metabolic phenotyping (food intake, energy expenditure, glucose metabolism), c-Fos neuronal activation Molecular metabolism High 30352741
2025 MRAP2 interacts with melatonin receptors MTNR1A and MTNR1B, inhibits their constitutive activity, and enhances maximal agonist potency. MRAP2 suppresses membrane trafficking of MTNR1A but promotes surface trafficking of MTNR1B. Co-immunoprecipitation, BiFC assay, GloSensor luminescence (Gi signaling), fixed-cell ELISA (surface expression) Frontiers in endocrinology Medium 40510472
2021 MRAP2 forms a symmetric antiparallel homodimer topology on the plasma membrane. Inversion of individual MRAP2 domains (N-terminal, transmembrane, C-terminal) via chimeric constructs shows proper dimer assembly but alters regulatory profile on MC4R surface expression and ligand-stimulated cAMP signaling, demonstrating functional importance of domain orientation within the dimer. Chimeric domain-inversion constructs, cell surface expression assays, cAMP signaling assays, homodimer characterization Frontiers in endocrinology Medium 34759891

Source papers

Stage 0 corpus · 51 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2009 MRAP and MRAP2 are bidirectional regulators of the melanocortin receptor family. Proceedings of the National Academy of Sciences of the United States of America 196 19329486
2013 Developmental control of the melanocortin-4 receptor by MRAP2 proteins in zebrafish. Science (New York, N.Y.) 136 23869017
2019 Loss-of-function mutations in MRAP2 are pathogenic in hyperphagic obesity with hyperglycemia and hypertension. Nature medicine 80 31700171
2017 MRAP2 regulates ghrelin receptor signaling and hunger sensing. Nature communications 65 28959025
2017 Regions of MRAP2 required for the inhibition of orexin and prokineticin receptor signaling. Biochimica et biophysica acta. Molecular cell research 57 28939058
2020 The GPCR accessory protein MRAP2 regulates both biased signaling and constitutive activity of the ghrelin receptor GHSR1a. Science signaling 50 31911434
2017 The interaction of MC3R and MC4R with MRAP2, ACTH, α-MSH and AgRP in chickens. The Journal of endocrinology 48 28512117
2020 Emerging roles of melanocortin receptor accessory proteins (MRAP and MRAP2) in physiology and pathophysiology. Gene 38 32679290
2016 Loss of Mrap2 is associated with Sim1 deficiency and increased circulating cholesterol. The Journal of endocrinology 36 27106110
2023 MRAP2 regulates energy homeostasis by promoting primary cilia localization of MC4R. JCI insight 30 36692018
2016 Copy number variation (CNV) analysis and mutation analysis of the 6q14.1-6q16.3 genes SIM1 and MRAP2 in Prader Willi like patients. Molecular genetics and metabolism 29 26795956
2019 Orange-spotted grouper melanocortin-4 receptor: Modulation of signaling by MRAP2. General and comparative endocrinology 27 31398355
2021 MRAP2 Interaction with Melanocortin-4 Receptor in SnakeHead (Channa argus). Biomolecules 25 33807040
2020 The Insulinostatic Effect of Ghrelin Requires MRAP2 Expression in δ Cells. iScience 21 32535024
2018 Overexpression of melanocortin 2 receptor accessory protein 2 (MRAP2) in adult paraventricular MC4R neurons regulates energy intake and expenditure. Molecular metabolism 21 30352741
2012 Melanocortin 2 receptor-associated protein (MRAP) and MRAP2 in human adrenocortical tissues: regulation of expression and association with ACTH responsiveness. The Journal of clinical endocrinology and metabolism 21 22419722
2019 Pharmacological modulation of MRAP2 protein on melanocortin receptors in the sea lamprey. Endocrine connections 20 30856611
2018 Evaluating the interactions between red stingray (Dasyatis akajei) melanocortin receptors and elephant shark (Callorhinchus milii) MRAP1 and MRAP2 following stimulation with either stingray ACTH(1-24) or stingray Des-Acetyl-αMSH: A pharmacological study in Chinese Hamster Ovary cells. General and comparative endocrinology 19 29524525
2016 Hypothesis and Theory: Revisiting Views on the Co-evolution of the Melanocortin Receptors and the Accessory Proteins, MRAP1 and MRAP2. Frontiers in endocrinology 18 27445982
2013 Mrap2: an accessory protein linked to obesity. Cell metabolism 18 24011068
2020 Study of LEP, MRAP2 and POMC genes as potential causes of severe obesity in Brazilian patients. Eating and weight disorders : EWD 17 32578125
2019 Analyzing the signaling properties of gar (Lepisosteus oculatus) melanocortin receptors: Evaluating interactions with MRAP1 and MRAP2. General and comparative endocrinology 16 31276671
2017 Analyzing the effects of co-expression of chick (Gallus gallus) melanocortin receptors with either chick MRAP1 or MRAP2 in CHO cells on sensitivity to ACTH(1-24) or ACTH(1-13)NH2: Implications for the avian HPA axis and avian melanocortin circuits in the hypothalamus. General and comparative endocrinology 16 28888694
2019 Pharmacological modulation of two melanocortin-5 receptors by MRAP2 proteins in zebrafish. Journal of molecular endocrinology 14 30400043
2014 Melanocortin receptor accessory protein 2 (MRAP2) interplays with the zebrafish melanocortin 1 receptor (MC1R) but has no effect on its pharmacological profile. General and comparative endocrinology 13 24709359
2022 MRAP2 inhibits β-arrestin recruitment to the ghrelin receptor by preventing GHSR1a phosphorylation. The Journal of biological chemistry 11 35605660
2020 Pharmacological properties of whale shark (Rhincodon typus) melanocortin-2 receptor and melancortin-5 receptor: Interaction with MRAP1 and MRAP2. General and comparative endocrinology 11 32213301
2024 MRAP2 Inhibits β-Arrestin-2 Recruitment to the Prokineticin Receptor 2. Current issues in molecular biology 9 38392222
2022 Determination of the Interaction and Pharmacological Modulation of MCHR1 Signaling by the C-Terminus of MRAP2 Protein. Frontiers in endocrinology 9 35311242
2022 Arginine 125 Is an Essential Residue for the Function of MRAP2. International journal of molecular sciences 9 36077245
2021 MC2R/MRAP2 activation could affect bovine ovarian steroidogenesis potential after ACTH treatment. Theriogenology 9 34425302
2025 Obesity-associated MRAP2 variants impair multiple MC4R-mediated signaling pathways. Human molecular genetics 8 39807633
2023 A novel pathogenic variant in MRAP2 in an obese patient with successful outcome of bariatric surgery. European journal of endocrinology 8 37888144
2021 Regulation of melanocortin-5 receptor pharmacology by two isoforms of MRAP2 in ricefield eel (Monopterus albus). General and comparative endocrinology 7 34653433
2021 Functional Characterization of the Internal Symmetry of MRAP2 Antiparallel Homodimer. Frontiers in endocrinology 6 34759891
2022 Reversion of MRAP2 Protein Sequence Generates a Functional Novel Pharmacological Modulator for MC4R Signaling. Biology 5 35741395
2021 Elucidation of the dimeric interplay of dual MRAP2 proteins in the zebrafish. Journal of cellular physiology 5 33559170
2019 MRAP2 regulates endometrial receptivity and function. Gene 5 30951854
2010 siRNA-mediated knockdown of the melanocortin 2 receptor accessory protein 2 (MRAP2) gene confers resistance to methylmercury on HEK293 cells. The Journal of toxicological sciences 5 21139347
2025 MRAP2 modifies the signaling and oligomerization state of the melanocortin-4 receptor. Nature communications 4 40998819
2024 The MRAP2 accessory protein directly interacts with melanocortin-3 receptor to enhance signaling. bioRxiv : the preprint server for biology 4 39574659
2022 Analyzing the Hypothalamus/Pituitary/Interrenal axis of the neopterygian fish, Lepisosteus oculatus: Co-localization of MC2R, MC5R, MRAP1, and MRAP2 in interrenal cells. General and comparative endocrinology 4 35447133
2021 Pharmacological properties of whale shark (Rhincodon typus) melanocortin-2 receptor and melancortin-5 receptor: Interaction with MRAP1 and MRAP2. General and comparative endocrinology 4 34607718
2025 The accessory protein MRAP2 directly interacts with melanocortin-3 receptor to enhance signaling. Science signaling 3 41401256
2023 Molecular and pharmacological analysis of the melanocortin-2 receptor and its accessory proteins Mrap1 and Mrap2 in a Squalomorph shark, the Pacific spiny dogfish. General and comparative endocrinology 2 37454980
2026 MRAP2 potentiates GPCR signaling by conserved mechanisms that are disrupted by obesity-associated genetic variants. Cell reports 1 41722048
2025 MRAP2 potentiates GPCR signaling by conserved mechanisms that are disrupted by obesity-associated genetic variants. bioRxiv : the preprint server for biology 1 41040264
2026 Association of Mutations in the Melanocortin-2 Receptor Accessory Protein 2 Gene (MRAP2) and Obesity: A Systematic Review and Meta-Analysis. International journal of molecular sciences 0 41596694
2026 Functional characterisation of obesity-associated MRAP2 variants on MC4R and GHSR signalling. Human molecular genetics 0 41758604
2025 Pharmacological modulation of MRAP2 protein on murine melatonin receptor signaling. Frontiers in endocrinology 0 40510472
2022 Pharmacology of orange-spotted grouper (Epinephelus coioides) melanocortin-5 receptor and its modulation by Mrap2. General and comparative endocrinology 0 36455644