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    Mol Cell Endocrinol. 2009 Mar 5;300(1-2):25-31. Epub 2008 Nov 6.

    Structure and function of the melanocortin2 receptor accessory protein (MRAP).

    Hinkle PM, Sebag JA.

    Source

    Department of Pharmacology and Physiology, University of Rochester Medical Center, Rochester, NY 14642, United States. patricia_hinkle@urmc.rochester.edu

    Abstract

    The melanocortin2 (MC2), or ACTH receptor, requires MC2 receptor accessory protein (MRAP) for function, and individuals lacking MRAP are ACTH-resistant and glucocorticoid-deficient. MRAP facilitates trafficking of the MC2 receptor to the plasma membrane and is absolutely required for ACTH binding and stimulation of cAMP. MRAP, which contains a single transmembrane domain, has a unique structure, an antiparallel homodimer. It can be isolated from the plasma membrane in a complex with the MC2 receptor. A short sequence just aminoterminal to the transmembrane domain of MRAP is essential for dual topology, while the transmembrane region is not; both are necessary for function. Deletion or alanine-substitution of other aminoterminal regions yields MRAP mutants that promote surface expression of the MC2 receptor but not receptor signaling. These results identify two distinct actions of MRAP: to permit trafficking of the MC2 receptor, and to allow surface receptor binding and signaling.

    PMID:
    19028547
    [PubMed - indexed for MEDLINE]
    PMCID: PMC2677758
    Free PMC Article

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