Journal article
Melanocortin Receptor Accessory Proteins (MRAPs): Functions in the melanocortin system and beyond
Biochimica et biophysica acta. Molecular basis of disease, Vol.1863(10 Pt A), pp.2462-2467
10/2017
DOI: 10.1016/j.bbadis.2017.05.008
PMID: 28499989
Abstract
G-protein coupled receptors (GPCRs) are regulated by numerous proteins including kinases, G-proteins, β-arrestins and accessory proteins. Several families of GPCR accessory proteins like Receptor Activity Modifying Proteins, Receptor Transporting Proteins and Melanocortin Receptor Accessory Proteins (MRAPs) have been identified as regulator of receptor trafficking, signaling and ligand specificity. The MRAP family contains two members, MRAP1 and MRAP2, responsible for the formation of a functional ACTH receptor and for the regulation of energy homeostasis respectively. Like all known GPCR accessory proteins, MRAPs are single transmembrane proteins, however, they form a unique structure since they assemble as an anti-parallel homodimer. Moreover, the accepted idea that MRAPs are specific regulators of melanocortin receptors was recently challenged by the discovery that MRAP2 inhibits the activity of prokineticin receptors. Recent studies are starting to explain the role of the unusual structure of MRAPs and to illustrate the importance of MRAP2 for the maintenance of both energy and glucose homeostasis. This article is part of a Special Issue entitled: Melanocortin Receptors - edited by Ya-Xiong Tao.
Details
- Title: Subtitle
- Melanocortin Receptor Accessory Proteins (MRAPs): Functions in the melanocortin system and beyond
- Creators
- Alix A J Rouault - University of Iowa, Carver College of Medicine, Department of Molecular Physiology and Biophysics, Fraternal Order of Eagle Diabetes Research Center, Iowa City, IA 52242, United StatesDinesh K Srinivasan - University of Iowa, Carver College of Medicine, Department of Molecular Physiology and Biophysics, Fraternal Order of Eagle Diabetes Research Center, Iowa City, IA 52242, United StatesTerry C Yin - University of Iowa, Carver College of Medicine, Department of Molecular Physiology and Biophysics, Fraternal Order of Eagle Diabetes Research Center, Iowa City, IA 52242, United StatesAbigail A Lee - University of Iowa, Carver College of Medicine, Department of Molecular Physiology and Biophysics, Fraternal Order of Eagle Diabetes Research Center, Iowa City, IA 52242, United StatesJulien A Sebag - University of Iowa, Carver College of Medicine, Department of Molecular Physiology and Biophysics, Fraternal Order of Eagle Diabetes Research Center, Iowa City, IA 52242, United States. Electronic address: Julien-sebag@uiowa.edu
- Resource Type
- Journal article
- Publication Details
- Biochimica et biophysica acta. Molecular basis of disease, Vol.1863(10 Pt A), pp.2462-2467
- DOI
- 10.1016/j.bbadis.2017.05.008
- PMID
- 28499989
- NLM abbreviation
- Biochim Biophys Acta Mol Basis Dis
- ISSN
- 0925-4439
- eISSN
- 1879-260X
- Publisher
- Netherlands
- Language
- English
- Date published
- 10/2017
- Academic Unit
- Molecular Physiology and Biophysics; Iowa Neuroscience Institute; Fraternal Order of Eagles Diabetes Research Center; Otolaryngology
- Record Identifier
- 9984070591902771
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