The palmitoylation or S-acylation of at least some G protein cu subuni
ts is a dynamic process that is regulated in vivo by the activation of
associated receptors. Highly purified, myristoylated G(i alpha 1) and
other G protein alpha subunits react spontaneously with palmitoyl-CoA
in vitro to form thioesterified proteins. This reaction requires nati
ve G(i alpha 1) and occurs exclusively at Cys(3), the same residue tha
t is palmitoylated in vivo. The reaction proceeds to completion, and i
ts rate is roughly equal to the rate of loss of palmitate observed in
pulse-chase experiments in vivo. The rate of autoacylation is signific
antly enhanced by the G protein py subunit complex. Autoacylation may
play a role in the dynamic thioesterification of some cellular protein
s.