G protein coupled receptors are involved in highly efficient and specific activation of signaling pathways. Yet, we do not fully understand the processes required to assemble the different partners of the GPCR signaling complex. In order to address this issue, we need to understand how receptors and their signaling -partners are synthesized, folded and regulated during quality control steps in order to generate functional proteins. Several molecular chaperones are involved in this process for most proteins, including GPCRs. Several membrane proteins require the assembly of different subunits to be functional. In recent years, GPCRs have been shown to form oligomers, which could be interpreted as subunits of a larger complex. Yet, those oligomers would not be functional without the association of other signaling partners; thus, there is a requirement for the specific assembly of the -different partners. In this chapter, we will cover some aspects of the current knowledge about how chaperones are involved in both the formation of GPCR oligomers and in the assembly of the receptors with their signaling complex components.