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Vol. 273, Issue 4, 1946-1950, January 23, 1998
From the Department of Pharmacology, College of Veterinary
Medicine, Cornell University, Ithaca, New York 14853
GTP-binding protein/transglutaminases (tissue
transglutaminases or TGases) have been implicated in a variety of
cellular processes including retinoic acid (RA)-induced apoptosis.
Recently, we have shown that RA activates TGases as reflected by
stimulated GTP binding, increased membrane association, and stimulated
phosphoinositide lipid turnover. This prompted us to search for
cellular proteins that bind TGases in a RA-stimulated manner. In this
report, we show that the eukaryotic initiation factor (eIF-5A), a
protein that is essential for cell viability, perhaps through effects on protein synthesis and/or RNA export, associates with the TGase in vivo. The interaction between eIF-5A and TGase is
specific for the GDP-bound form of the TGase and is not detected when
the TGase is pre-loaded with GTP
S. The TGase-eIF-5A interaction also is promoted by Ca2+, Mg2+, and RA treatment of
HeLa cells. In the presence of retinoic acid, millimolar levels of
Ca2+ are no longer required for the TGase-eIF-5A
interaction. Nocodazole treatment, which blocks the cell cycle at
mitosis (M phase), strongly inhibits the interaction between eIF-5A and
cytosolic TGase. The interaction between TGase and eIF-5A and its
sensitivity to the nucleotide-occupied state of the TGase provides a
potentially interesting connection between RA signaling and protein
synthesis and/or RNA trafficking activities.
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