[The role of molecular chaperones in the assembly of heterotrimeric G proteins].
Extracellular signals received by G protein-coupled receptors (GPCRs) are transduced into intracellular responses following the activation of heterotrimeric G proteins. As their names suggests, they are composed of three subunits, Galpha and Gbetagamma, the latter being effectively treated as a single entity. The Gbetagamma dimer is assembled with the aid of a number of molecular chaperones in a tightly regulated process. The folding of nascent Gbeta1 is favoured by cellular chaperones such as PhLP-1 and CCT and the ER-resident protein DRiP78 plays an important role in the stability of nascent Ggamma2 subunits. However, much work remains to be done to completely understand the mechanisms underlying assembly of the heterotrimer.
Département de biochimie, Université de Montréal, CP 6128, succursale centre-ville, Montréal, Québec H3C 3J7 Canada.
Mélanie
M
Robitaille
Denis J
DJ
Dupré
Terence E
TE
Hébert
D044385:GTP-Binding Protein alpha Subunits / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000378:metabolism; D020962:Heterotrimeric GTP-Binding Proteins / Q000096:biosynthesis*; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism
D044385:GTP-Binding Protein alpha Subunits; D018832:Molecular Chaperones; D019204:GTP-Binding Proteins; D020962:Heterotrimeric GTP-Binding Proteins