Journal article
Structure and function of the melanocortin2 receptor accessory protein (MRAP)
Molecular and cellular endocrinology, Vol.300(1-2), pp.25-31
03/05/2009
DOI: 10.1016/j.mce.2008.10.041
PMID: 19028547
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.
Details
- Title: Subtitle
- Structure and function of the melanocortin2 receptor accessory protein (MRAP)
- Creators
- Patricia M HinkleJulien A Sebag
- Resource Type
- Journal article
- Publication Details
- Molecular and cellular endocrinology, Vol.300(1-2), pp.25-31
- DOI
- 10.1016/j.mce.2008.10.041
- PMID
- 19028547
- NLM abbreviation
- Mol Cell Endocrinol
- ISSN
- 0303-7207
- eISSN
- 1872-8057
- Publisher
- Elsevier Ireland Ltd
- Language
- English
- Date published
- 03/05/2009
- Academic Unit
- Molecular Physiology and Biophysics; Iowa Neuroscience Institute
- Record Identifier
- 9984025589902771
Metrics
14 Record Views