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MBC in Press, published online ahead of print December 19, 2007
Mol. Biol. Cell 10.1091/mbc.E07-09-0893

A more recent version of this article appeared on March 1, 2008
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Submitted on September 12, 2007
Revised on November 16, 2007
Accepted on December 12, 2007

Caenorhabditis elegans mboa-7, a Member of the MBOAT Family, Is Required for Selective Incorporation of Polyunsaturated Fatty Acids into Phosphatidylinositol

Hyeon-Cheol Lee,* Takao Inoue,*{dagger} Rieko Imae,* Nozomu Kono,* Shinichiro Shirae,* Shinji Matsuda,* Keiko Gengyo-Ando,{dagger}{ddagger} Shohei Mitani,{dagger}{ddagger} and Hiroyuki Arai*{dagger}

*Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo 113-0033, Japan; {ddagger}Department of Physiology, Tokyo Women’s Medical University, School of Medicine, Tokyo 162-8666, Japan; {dagger}CREST, Japan Science and Technology Agency (JST), Kawaguchi, Saitama 332-0012, Japan

Monitoring Editor: Reid Gilmore

Phosphatidylinositol (PI) is a component of membrane phospholipids and functions both as a signaling molecule and as a compartment-specific localization signal in the form of polyphosphoinositides. Arachidonic acid (AA) is the predominant fatty acid in the sn-2 position of PI in mammals. LysoPI acyltransferase (LPIAT) is thought to catalyze formation of AA-containing PI; however, the gene that encodes this enzyme has not yet been identified. In this study, we established a screening system to identify genes required for utilization of exogenous polyunsaturated fatty acids (PUFAs) in C. elegans. In C. elegans, eicosapentaenoic acid (EPA) instead of AA is the predominant fatty acid in PI. We showed that an uncharacterized gene, which we named mboa-7, is required for incorporation of PUFAs into PI. Incorporation of exogenous PUFA into PI of the living worms and LPIAT activity in the microsomes were greatly reduced in mboa-7 mutants. Furthermore, the membrane fractions of transgenic worms expressing recombinant MBOA-7 and its human homolog exhibited remarkably increased LPIAT activity. mboa-7 encodes a member of the membrane-bound O-acyltransferase family, suggesting that mboa-7 is LPIAT. Finally, mboa-7 mutants had significantly lower EPA levels in PI and exhibited larval arrest and egg-laying defects.

Address correspondence to: Takao Inoue (akao{at}mol.f.u-tokyo.ac.jp) or Hiroyuki Arai (harai{at}mol.f.u-tokyo.ac.jp)




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