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interaction of RAMP2 or RAMP3 with CLR induces conformational variation in the juxtamembrane region, yielding distinct binding pockets, probably via an allosteric mechanism.
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the AM system is widely expressed in human thymus from newborns; both AM1 receptor components CLR and RAMP2, but not RAMP3, are not associated with the plasma membrane of TECs and thymocytes but are located intracellularly, notably in the nucleus
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Data suggest isoforms of RAMP modulate accessibility of peptides to residues situated on CALCRL (calcitonin receptor-like receptor) N-terminal domain; RAMP3/RAMP2/RAMP1 appear to alter accessibility of specific residues at CALCRL-RAMP interface.
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The expression of RAMP3 is downregulated in the fetal lung with increasing gestational age.
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the RAMP3 TMD participates in the negative regulation of CLR/RAMP3 internalization.
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Data show that LOXL2 and RAMP3 are strongly coexpressed in human colon, breast, and gastric carcinomas but not in normal colon or gastric epithelial cells.
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This study provides insight into the role of three amino acid changes in human RAMP3.
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Morphological fluorescence techniques, bioluminescence resonance energy transfer, and bimolecular fluorescence complementation analysis demonstrate that the secretin receptor associates specifically with RAMP3, but not with RAMP1 or RAMP2.
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Receptor activity modifying proteins interaction with human and porcine calcitonin receptor-like receptor (CRLR) in HEK-293 cells
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results show the presence of calcitonin receptor-like receptor and receptor activity-modifying proteins in middle meningeal, middle cerebral, pial, and superficial temporal vessels
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Co-expression of calcitonin receptors (CT) lacking a portion of domain 1 with receptor activity-modifying protein (RAMP) 1, 2, or 3 appears to produce functional CT-(8-32)-sensitive adrenomedullin receptors.
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Data found that expressions of RAMP1, RAMP2 and RAMP3 mRNAs increased with the worsening of heart function, but the expressions of RAMP1 and RAMP2 mRNA decreased at level IV of heart failure.
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RAMP3 interacts with N-ethylmaleimide-sensitive factor to cause the change in trafficking
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results, using both endogenous and overexpressed cellular models, indicate a novel function for NHERF-1 and RAMP3 in the internalization of the adrenomedullin receptor and suggest additional regulatory mechanisms for receptor trafficking
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the respective C-tails of hRAMP2 and -3 differentially affect hCRLR surface delivery and internalization
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This study reveals important functionality of the RAMP C-terminal domain and identifies key differences in the role of the RAMP C terminus for calcitonin receptor versus calcitonin receptor-like receptor-based receptors.
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Identification of RAMP3 residues for adrenomedjullin receptors are reported.
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The His residues of hRAMP2 and -3 differentially govern adrenomedullin receptor function.
