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A more recent version of this article appeared on September 1, 2002
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Submitted on February 21, 2002
Revised on June 12, 2002
Accepted on June 28, 2002
1 Department of Medicine, Cell Biology and Pharmacology, NYU School of Medicine
2 The Gladstone Institute of Cardiovascular Research, UCSF
* Corresponding author. E-mail address: philim01{at}med.nyu.edu.
Membrane targeting of G-protein 
ß
heterotrimers was investigated in live cells using G and G subunits tagged with spectral mutants of GFP. Unlike Ras proteins, Gß contains a single targeting signal, the CAAX motif, that directed the dimer to the endoplasmic reticulum (ER). Endomembrane localization of farnesylated G1, but not geranylgeraylated G2, required carboxyl methylation. Targeting of the heterotrimer to the plasma membrane (PM) required co-expression of all three subunits, combining the CAAX motif of G with the fatty acyl modifications of G. G associated with Gß on the Golgi and palmitoylation of G was required for translocation of the heterotrimer to the PM. Thus two separate signals, analogous to the dual-signal targeting mechanism of Ras proteins, cooperate to target heterotrimeric G-proteins to the PM via the endomembrane.
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