PMC:4504005 / 4525-5907
Annnotations
{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/4504005","sourcedb":"PMC","sourceid":"4504005","source_url":"https://www.ncbi.nlm.nih.gov/pmc/4504005","text":"CGRP, AM, and AM2 binding to their cognate class B receptor, the calcitonin receptor-like receptor (CLR), is dependent on association of CLR with one of three accessory membrane proteins that determine ligand selectivity; receptor activity-modifying proteins (RAMPs) 1, 2, or 3 (Hong et al., 2012; McLatchie et al., 1998). RAMPs have an ECD of about 100 amino acids and a single TM segment (Parameswaran and Spielman, 2006). CLR:RAMP1 is a CGRP receptor, CLR:RAMP2 preferentially recognizes AM and is called the AM1 receptor, and CLR:RAMP3 binds both AM and AM2 with high affinities and is called the AM2 receptor. Amy by itself has a low affinity for the class B CT receptor (CTR); however, when CTR associates with any of the RAMPs, its affinity for Amy is markedly increased (Christopoulos et al., 1999; Poyner et al., 2002). CTR alone is the receptor for CT. Thus, the RAMPs profoundly alter the behavior of CLR and CTR. Although RAMPs are best characterized for their effects on CLR/CTR, they also interact with several other class B GPCRs and with certain class A/Rhodopsin and class C/Glutamate family GPCRs, making it particularly important to understand the molecular basis for RAMP actions (Bouschet et al., 2005; Lenhart et al., 2013; Wootten et al., 2010). 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