By the process of dimerization, we found that 5TM mutant proteins such as GHS-R1b maintain full length GPCRs such as GHS-R1a in the ER. As a result, fewer mature GHS-R1a gets to the cell surface and the ability of the cell to respond to ghrelin is attenuated.
Over recent years it has become clear that several disease states associated with abnormal hormonal responses are associated with the presence of truncated mutant GPCRs which interfere with the normal functioning of the hormone receptor. By using pharamcological tools, it is possible to 'persuade' these abnormal proteins to leave the ER, but such tools are rare given the large number of truncated/mutant GPCRs that exist.
