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.
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Related Subject Headings
- Signal Transduction
- Protein Prenylation
- GTP-Binding Proteins
- Biochemistry & Molecular Biology
- Animals
- 3101 Biochemistry and cell biology
- 1116 Medical Physiology
- 0601 Biochemistry and Cell Biology
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Signal Transduction
- Protein Prenylation
- GTP-Binding Proteins
- Biochemistry & Molecular Biology
- Animals
- 3101 Biochemistry and cell biology
- 1116 Medical Physiology
- 0601 Biochemistry and Cell Biology