The role of prenylation in G-protein assembly and function.
Journal Article (Journal Article;Review)
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.
Full Text
Duke Authors
Cited Authors
- Higgins, JB; Casey, PJ
Published Date
- September 1996
Published In
Volume / Issue
- 8 / 6
Start / End Page
- 433 - 437
PubMed ID
- 8958445
International Standard Serial Number (ISSN)
- 0898-6568
Digital Object Identifier (DOI)
- 10.1016/s0898-6568(96)00071-x
Language
- eng
Conference Location
- England