TY - JOUR
T1 - Disruption of the Saccharomyces cerevisiae homologue to the murine fatty acid transport protein impairs uptake and growth on long-chain fatty acids
AU - Færgeman, Nils J.
AU - DiRusso, Concetta C.
AU - Elberger, Andrea
AU - Knudsen, Jens
AU - Black, Paul N.
PY - 1997/3/28
Y1 - 1997/3/28
N2 - The yeast Saccharomyces cerevisiae is able to utilize exogenous fatty acids for a variety of cellular processes including β-oxidation, phospholipid biosynthesis, and protein modification. The molecular mechanisms that govern the uptake of these compounds in S. cerevisiae have not been described. We report the characterization of FAT1, a gene that encodes a putative membrane-bound long-chain fatty acid transport protein (Fat1p). Fat1p contains 623 amino acid residues that are 33% identical and 54% with similar chemical properties as compared with the fatty acid transport protein FATP described in 3T3-L1 adipocytes (Schaffer and Lodish (1994) Cell 79, 427- 436), suggesting a similar function. Disruption of FAT1 results in 1) an impaired growth in YPD medium containing 25 μM cerulenin and 500 μM fatty acid (myristate (C(14:0)), palmitate (C(16:0)), or oleate (C(18:1))); 2) a marked decrease in the uptake of the fluorescent long-chain fatty acid analogue boron dipyrromethene difluoride dodecanoic acid (BODIPY-3823); 3) a reduced rate of exogenous oleate incorporation into phospholipids; and 4) a 2-3-fold decrease in the rates of oleate uptake. These data support the hypothesis that Fat1p is involved in long-chain fatty acid uptake and may represent a long-chain fatty acid transport protein.
AB - The yeast Saccharomyces cerevisiae is able to utilize exogenous fatty acids for a variety of cellular processes including β-oxidation, phospholipid biosynthesis, and protein modification. The molecular mechanisms that govern the uptake of these compounds in S. cerevisiae have not been described. We report the characterization of FAT1, a gene that encodes a putative membrane-bound long-chain fatty acid transport protein (Fat1p). Fat1p contains 623 amino acid residues that are 33% identical and 54% with similar chemical properties as compared with the fatty acid transport protein FATP described in 3T3-L1 adipocytes (Schaffer and Lodish (1994) Cell 79, 427- 436), suggesting a similar function. Disruption of FAT1 results in 1) an impaired growth in YPD medium containing 25 μM cerulenin and 500 μM fatty acid (myristate (C(14:0)), palmitate (C(16:0)), or oleate (C(18:1))); 2) a marked decrease in the uptake of the fluorescent long-chain fatty acid analogue boron dipyrromethene difluoride dodecanoic acid (BODIPY-3823); 3) a reduced rate of exogenous oleate incorporation into phospholipids; and 4) a 2-3-fold decrease in the rates of oleate uptake. These data support the hypothesis that Fat1p is involved in long-chain fatty acid uptake and may represent a long-chain fatty acid transport protein.
UR - http://www.scopus.com/inward/record.url?scp=0030889638&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0030889638&partnerID=8YFLogxK
U2 - 10.1074/jbc.272.13.8531
DO - 10.1074/jbc.272.13.8531
M3 - Article
C2 - 9079682
AN - SCOPUS:0030889638
SN - 0021-9258
VL - 272
SP - 8531
EP - 8538
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 13
ER -