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

Published

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

Pubmed Central 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