Chaperones contribute to G protein coupled receptor oligomerization but do not participate in assembly of the G protein with the receptor signaling complex

摘要

BackgroundPrevious studies have demonstrated that seven transmembrane receptors (7TM-Rs) can associate with various chaperones to control their maturation and export. It has been shown for a few years now that 7TM-Rs can form homo or heterooligomeric complexes. Due to the difficulty to study heterooligomers in a context devoid of homooligomers signaling, very little is known on heterooligomerization. β2AR-AT1R receptor complexes have been found on cells and ligand activation of one receptor affects signaling of the partner. Yet, very little is known about the mechanisms linking those receptors together. We propose to examine the role of chaperones in the maturation of homo- and heterodimers of the β2AR and AT1R. It would not be surprising that strict cellular mechanisms exist to ensure that only properly folded receptors are inserted into the plasma membrane.