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J Biol Chem, Vol. 273, Issue 44, 28642-28650, October 30, 1998
From the Center for Cardiovascular Research, Department of Internal
Medicine and the Department of Molecular Biology and Pharmacology,
Washington University School of Medicine, St. Louis, Missouri
63110-1010
The murine fatty acid transport protein (FATP)
was identified on the basis of its ability to facilitate uptake of long
chain fatty acids (LCFAs) when expressed in mammalian cells. To
delineate FATP domains important for transport function, we cloned the
human heart FATP ortholog. Comparison of the human, murine, and yeast amino acid sequences identified a highly conserved motif,
IYTSGTTGXPK, also found in a number of proteins that form
adenylated intermediates. We demonstrate that depletion of
intracellular ATP dramatically reduces FATP-mediated LCFA uptake.
Furthermore, wild-type FATP specifically binds
[
-32P]azido-ATP. Introduction of a serine to alanine
substitution (S250A) in the IYTSGTTGXPK motif produces an
appropriately expressed and metabolized mutant FATP that demonstrates
diminished LCFA transport function and decreased
[-32P]azido-ATP binding. These results are consistent
with a mechanism of action for FATP involving ATP binding that is
dependent on serine 250 of the IYTSGTTGXPK motif.
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