Lipid metabolismFatty acid transport proteinsGimeno, Ruth EAuthor Information Department of Cardiovascular and Metabolic Diseases, Wyeth Research, Cambridge, Massachusetts, USA Correspondence to Ruth E. Gimeno Department of Cardiovascular and Metabolic Diseases, Wyeth Research, 200 Cambridge Park Drive, Cambridge, MA 02140, USA Tel: +1 617 665 5423; fax: +1 617 665 5499; e-mail: [email protected] Current Opinion in Lipidology: June 2007 - Volume 18 - Issue 3 - p 271-276 doi: 10.1097/MOL.0b013e3281338558 Buy Metrics Abstract Purpose of review Fatty acid transport proteins are a family of proteins involved in fatty acid uptake and activation. This review summarizes recent progress in elucidating the function of fatty acid transport proteins. Recent findings Recent experiments clearly establish FATP1 as a regulated fatty acid transporter in both adipose tissue and muscle with important roles in energy homeostasis, thermogenesis and insulin resistance. Knockout of FATP5 in mice show it to be a bifunctional protein required for both hepatic fatty acid uptake and bile acid reconjugation. The most striking phenotype of FATP4 deletion is a defect in skin homeostasis, which may be due to its very long chain acyl-coenzyme A synthetase activity. Fatty acid transport proteins are increasingly being recognized as multifunctional proteins that can mediate the uptake of fatty acids as well as catalyze the formation of coenzyme A derivatives using long-chain and very-long chain fatty acids, bile acids and bile acid precursors as substrates. Summary Modulation of fatty acid transport protein function can result in altered energy homeostasis and insulin sensitivity, defective skin homeostasis, and altered bile acid metabolism. Both fatty acid uptake and enzymatic activity of fatty acid transport proteins likely contribute to these phenotypes. Future studies are needed to better understand the molecular mechanism of fatty acid transport protein function and the physiological role of FATP2, FATP3, and FATP6. © 2007 Lippincott Williams & Wilkins, Inc.