ArticleThe Journal of biological chemistry2022
MRAP2 inhibits β-arrestin recruitment to the ghrelin receptor by preventing GHSR1a phosphorylation.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Attractin-like protein 1 is an essential partner of MC4R to regulate body weight.Nature communications · 2026Article
- Activation of the nucleus nuclear factor erythroid 2-related factor 2ghrelin/growth hormone secretagogue receptor 1a signaling by Yueju pill confers cardioprotective and antidepressant effects.Journal of traditional Chinese medicine = Chung i tsa chih ying wen pan · 2026Article
- Cellular signatures of melanocortin pathway genes across the locus coeruleus.Acta neuropathologica communications · 2026Article
- Functional characterisation of obesity-associated MRAP2 variants on MC4R and GHSR signalling.Human molecular genetics · 2026Article
- MRAP2 potentiates GPCR signaling by conserved mechanisms that are disrupted by obesity-associated genetic variants.bioRxiv : the preprint server for biology · 2025Article
- MRAP2 modifies the signaling and oligomerization state of the melanocortin-4 receptor.Nature communications · 2025Article
- Pharmacological modulation of MRAP2 protein on murine melatonin receptor signaling.Frontiers in endocrinology · 2025Article
- Syndecans modulate ghrelin receptor signaling.Journal of molecular endocrinology · 2025Article
- MRAP2 Inhibits β-Arrestin-2 Recruitment to the Prokineticin Receptor 2.Current issues in molecular biology · 2024Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The melanocortin receptor accessory protein 2 (MRAP2) is essential for several physiological functions of the ghrelin receptor growth hormone secretagogue receptor 1a (GHSR1a), including increasing appetite and suppressing insulin secretion. In the absence of MRAP2, GHSR1a displays high constitutive activity and a weak G-protein-mediated response to ghrelin and readily recruits β-arrestin. In the presence of MRAP2, however, G-protein-mediated signaling via GHSR1a is strongly dependent on ghrelin stimulation and the recruitment of β-arrestin is significantly diminished. To better understand how MRAP2 modifies GHSR1a signaling, here we investigated the role of several phosphorylation sites within the C-terminal tail and third intracellular loop of GHSR1a, as well as the mechanism behind MRAP2-mediated inhibition of β-arrestin recruitment. We show that Ser
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.