The role of prenylation in G-protein assembly and function.
Heterotrimeric guanine nucleotide-binding regulatory proteins (G-proteins) are vital components of numerous signal transduction pathways, including sensory and hormonal response systems. G-proteins transduce signals from heptahelical transmembrane receptors to downstream effectors. The localization of a G-protein to the plasma membrane, as well as its interaction with the appropriate receptor and effector, are essential for its function. In addition, the association of a G-protein's subunits to form its trimer is required for interaction with its receptor. The G-protein gamma subunits (G gamma) are subject to a set of carboxyl-terminal processing events that include prenylation of a cysteine, proteolysis, and methylation. Recent advances which elucidate the contributions that the post-translational modifications of the G gamma subunit have on the assembly, membrane association, and function of the G-protein trimer reveal that these modifications are required for important protein-protein, in addition to membrane-protein, interactions.
Higgins
J B
JB
Department of Molecular Cancer Biology, Duke University Medical Center, Durham, NC 27710-3686, USA.
Casey
P J
PJ
D000818:Animals; D019204:GTP-Binding Proteins / Q000096:biosynthesis*; D017368:Protein Prenylation / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology*
D019204:GTP-Binding Proteins