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Regions of melanocortin 2 (MC2) receptor accessory protein necessary for dual topology and MC2 receptor trafficking and signaling
Journal article   Open access   Peer reviewed

Regions of melanocortin 2 (MC2) receptor accessory protein necessary for dual topology and MC2 receptor trafficking and signaling

Julien A Sebag and Patricia M Hinkle
The Journal of biological chemistry, Vol.284(1), pp.610-618
01/02/2009
DOI: 10.1074/jbc.M804413200
PMCID: PMC2610514
PMID: 18981183
url
https://doi.org/10.1074/jbc.M804413200View
Published (Version of record) Open Access

Abstract

MRAP, melanocortin 2 (MC2) receptor accessory protein, is required for trafficking by the MC2 (ACTH) receptor. MRAP is a single transmembrane protein that forms highly unusual antiparallel homodimers. We used molecular complementation to ask where MRAP achieves dual topology. Fragments of yellow fluorescent protein (YFP) were fused to the NH2 or COOH terminus of MRAP such that YFP fluorescence could occur only in antiparallel homodimers; fluorescence was present in the endoplasmic reticulum. MRAP retained dual topology after deletion of most of the amino terminus. In contrast, deletion of residues 31-37, just NH2-terminal to the transmembrane domain, forced MRAP into a single Nexo/Ccyt orientation and blocked its ability to promote MC2 receptor trafficking and homodimerize. When the transmembrane domain of MRAP was replaced with the corresponding region from RAMP3, dual topology was retained but MRAP was inactive. Insertion of MRAP residues 29-37 conferred dual topology to RAMP3, normally in an Nexo/Ccyt orientation. When expressed with MRAPDelta1-30, MRAPDelta10-20, or MRAPDelta21-30, MC2 receptor was localized on the plasma membrane but unable to respond to ACTH. Residues 18-21 of MRAP were critical; MC2 receptor expressed with MRAP(18-21A) localized to the plasma membrane but did not bind 125I-ACTH or increase cAMP in response to ACTH. A newly identified MRAP homolog, MRAP2, lacks amino acids 18LDYI21 of MRAP and, like MRAP(18-21A), allows MC2 receptor trafficking but not signaling. MRAP2 with an LDYI insertion functions like MRAP. These results demonstrate that MRAP not only facilitates MC2 receptor trafficking but also allows properly localized receptor to bind ACTH and consequently signal.
Cricetulus Humans Endoplasmic Reticulum - metabolism Protein Transport - physiology Cell Membrane - genetics Intracellular Signaling Peptides and Proteins - metabolism Adrenocorticotropic Hormone - genetics Recombinant Fusion Proteins - metabolism Receptor, Melanocortin, Type 2 - metabolism Receptor, Melanocortin, Type 2 - genetics Receptor Activity-Modifying Protein 3 Cell Membrane - metabolism Membrane Proteins - metabolism Dimerization Intracellular Signaling Peptides and Proteins - genetics Adrenocorticotropic Hormone - metabolism CHO Cells Cricetinae Receptor Activity-Modifying Proteins - metabolism Endoplasmic Reticulum - genetics Membrane Proteins - genetics Animals Receptor Activity-Modifying Proteins - genetics Recombinant Fusion Proteins - genetics Signal Transduction - physiology Mice Protein Structure, Tertiary - physiology

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