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J. Biol. Chem., Vol. 269, Issue 7, 4713-4716, Feb, 1994
H Hallak, L Muszbek, M Laposata, E Belmonte, LF Brass and DR Manning
The alpha subunits of GTP-binding regulatory proteins (G proteins) are
subject to lipid modifications required for anchorage to membrane and/or
interactions with other proteins. With the knowledge that alpha subunits
are palmitoylated, which we demonstrate here for human platelets, we sought
to determine whether these subunits also bind arachidonate and myristate in
a covalent, post-translational manner. All alpha subunits examined were
found to incorporate radioactivity upon incubation of human platelets with
[3H]palmitate, [3H]arachidonate, and [3H]myristate. The identity of
[3H]palmitate and [3H]arachidonate as covalently bound fatty acids was
confirmed by high pressure liquid chromatography following alkaline
methanolysis. With [3H]myristate, however, the bound fatty acid proved to
be [3H]palmitate, presumably generated by a 2-carbon chain elongation.
Protein-bound [3H]palmitate and [3H]arachidonate were released by
hydroxylamine at neutral pH, implying a thioester linkage between protein
and fatty acid. Thus, post-translational modifications of G protein alpha
subunits include palmitoylation and arachidonoylation, but not
myristoylation. Given the different physical properties of saturated and
unsaturated fatty acids and the large-scale release of arachidonate during
platelet activation, changes in arachidonate incorporation may serve as an
important regulator of alpha subunit function.
Covalent binding of arachidonate to G protein alpha subunits of human platelets
Department of Pharmacology, University of Pennsylvania School of Medicine, Philadelphia 19104.
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