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J Biol Chem, Vol. 274, Issue 5, 2880-2884, January 29, 1999
§,§,§,§,§
From the Rab proteins play a crucial role in the
trafficking of intracellular vesicles. Rab proteins are GTPases that
cycle between an inactive GDP-bound form and an active GTP-bound
conformation. A prerequisite to Rab activation by GTP loading is its
post-translational modification by the addition of geranylgeranyl
moieties to highly conserved C-terminal cysteine residues. We examined
the effect of insulin on the activity of geranylgeranyltransferase II
(GGTase II) in 3T3-L1 fibroblasts and adipocytes. In fibroblasts,
insulin increased the enzymatic activity of GGTase II 2.5-fold after
1 h of incubation, an effect that is blocked by perillyl alcohol, an inhibitor of prenyltransferases, but not by the
geranylgeranyltransferase I inhibitor, GGTI-298, or the
farnesyltransferase inhibitor, Research Service, Veterans Affairs Medical
Center, Denver, Colorado 80220, the § Department of
Medicine, University of Colorado Health Sciences Center,
Denver, Colorado 80220, and ¶ INSERM U145, Faculty of Medicine,
06107 Nice, France
-hydroxyfarnesylphosphonic acid. Concomitantly, insulin stimulated the phosphorylation of the GGTase II -subunit without any effect on the GGTase II
-subunit. At the same time, insulin also increased the amounts of
geranylgeranylated Rab-3 in 3T3-L1 fibroblasts from 44 ± 1.2% in
control cells to 63 ± 3.8 and 64 ± 6.1% after 1 and
24 h of incubation, respectively. In adipocytes, insulin increased
the amounts of geranylgeranylated Rab-4 from 38 ± 0.6% in
control cells to 56 ± 1.7 and 60 ± 2.6% after 1 and
24 h of incubation, respectively. In both fibroblasts and
adipocytes, the presence of perillyl alcohol blocked the ability of
insulin to increase geranylgeranylation of Rab-4, whereas GGTI-298 and
-hydroxyfarnesylphosphonic acid were without effect, indicating that
insulin activates GGTase II. In summary, insulin promotes phosphorylation and activation of GGTase II in both 3T3 L1 fibroblasts and adipocytes and increases the amounts of geranylgeranylated Rab-3
and Rab-4 proteins.
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