Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2008189 | Peptides | 2005 | 10 Pages |
Abstract
The pigmentary actions of the melanocortins are mediated by the melanocortin-1 receptor (MC1R), a seven transmembrane domains receptor positively coupled to Gs and the cAMP cascade. In order to define the structure–function relationships of potentially relevant domains in MC1R, particularly its C-terminal cytosolic tail, we generated and analyzed several variants with C-terminal deletions, as well as point mutants in selected residues of the human MC1R. We show that the MC1R C-terminal pentapeptide is essential for proper receptor expression on the plasma membrane, and that residues Thr314, Cys315 and Trp317 are at least partially responsible for this effect.
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Biochemistry
Authors
J. Sánchez-Más, B.L. Sánchez-Laorden, L.A. Guillo, C. Jiménez-Cervantes, J.C. García-Borrón,