Disruption of the Saccharomyces cerevisiae homologue to the murine fatty acid transport protein impairs uptake and growth on long-chain fatty acids

Nils J. Færgeman, Concetta C. DiRusso, Andrea Elberger, Jens Knudsen, Paul N. Black

Research output: Contribution to journalArticle

124 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)8531-8538
Number of pages8
JournalJournal of Biological Chemistry
Volume272
Issue number13
DOIs
StatePublished - Mar 28 1997

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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