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Papers In Press, published online ahead of print December 15, 2005
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Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110
Corresponding Author: jschaff{at}wustl.edu
The fatty acid transport (FATP) and long chain acyl CoA synthetase (ACSL) proteins have been shown to play a role in facilitating long chain fatty acid transport in mammalian cells under physiologic conditions. The involvement of both FATP and ACSL proteins is consistent with the model of vectorial acylation in which fatty acid transport is coupled to esterification. The present study was undertaken to determine whether the functions of these proteins are coordinated through a protein-protein interaction that might serve as a point of regulation for cellular fatty acid transport. We demonstrate for the first time that FATP1 and ACSL1 co-immunoprecipitate in 3T3-L1 adipocytes, indicating that these proteins form an oligomeric complex. Efficiency of FATP1 and ACSL1 co-immunoprecipitation is unaltered by acute insulin treatment, which stimulates fatty acid uptake, or by treatment with isoproterenol, which decreases fatty acid uptake and stimulates lipolysis. Moreover, inhibition of ACSL1 activity in adipocytes impairs fatty acid uptake, suggesting that esterification is essential for fatty acid transport. Taken together, our findings suggest that a constitutive interaction between FATP1 and ACSL1 contributes to efficient cellular uptake of long chain fatty acids in adipocytes through vectorial acylation.
Revised on December 14, 2005
Accepted on December 14, 2005
Fatty acid transport protein 1 and long chain acyl CoA synthetase 1 interact in adipocytes
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