Membrane orientation and oligomerization of the melanocortin receptor accessory protein 2 [Metabolism]

In this study, we demonstrate that the conserved polybasic motif that dictates the membrane topology and dimerization of MRAP1 does not control the membrane orientation and dimerization of MRAP2. We also show that MRAP2 dimerizes through its transmembrane domain and can form higher-order oligomers that arrange MRAP2 monomers in a parallel orientation. Investigating the molecular details of MRAP2 structure is essential for understanding the mechanism by which it regulates G protein–coupled receptors and will aid in elucidating the pathways involved in metabolic dysfunction.

Source: Journal of Biological Chemistry - November 27, 2020 Category: Chemistry Authors: Valerie Chen, Antonio E. Bruno, Laura L. Britt, Ciria C. Hernandez, Luis E. Gimenez, Alys Peisley, Roger D. Cone, Glenn L. Millhauser Tags: Metabolism Source Type: research