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Cell Signal. 1996 Sep;8(6):433-7.

The role of prenylation in G-protein assembly and function.

Author information

1
Department of Molecular Cancer Biology, Duke University Medical Center, Durham, NC 27710-3686, USA.

Abstract

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.

PMID:
8958445
DOI:
10.1016/s0898-6568(96)00071-x
[Indexed for MEDLINE]

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