Receptor-activity-modifying proteins (RAMPs) with single transmembrane domains define the function of two G-protein-coupled receptors of the B family. Cell-surface complexes of human RAMP1 (hRAMP1) and human calcitonin (CT) receptor isotype 2 (hCTR2) or rat CT-receptor-like receptor (rCRLR) have now been identified through protein cross-linking, co-immunoprecipitation and confocal microscopy. They are two distinct CT-gene-related peptide (CGRP) receptors coupled to cAMP production and pharmacologically distinguished by the CT and CGRP antagonists salmon CT(8-32) and human or rat CGRP(8-37). Thus direct molecular interactions of hRAMP1 with hCTR2 or rCRLR are required for CGRP recognition. hCTR2, moreover, adopts non-traditional functions through its association with hRAMP1.
Receptor-activity-modifying protein 1 forms heterodimers with two G-protein-coupled receptors to define ligand recognition
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Kerstin LEUTHÄUSER, Remo GUJER, Amaya ALDECOA, R. ANNE McKINNEY, Roman MUFF, Jan A. FISCHER, Walter BORN; Receptor-activity-modifying protein 1 forms heterodimers with two G-protein-coupled receptors to define ligand recognition. Biochem J 15 October 2000; 351 (2): 347–351. doi: https://doi.org/10.1042/bj3510347
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