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J. Lipid Res.
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A more recent version of this article appeared on September 1, 2006

Papers In Press, published online ahead of print June 2, 2006
J. Lipid Res., doi:10.1194/jlr.M600172-JLR200
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Submitted on April 13, 2006
Revised on May 24, 2006
Accepted on June 1, 2006

Co-localization of SCD1 and DGAT2: implying preference for endogenous monounsaturated fatty acids in triglyceride synthesis

Weng Chi Man, Makoto Miyazaki, KiKi Chu, and James Ntambi

Biochemsitry, University of Wisconsin-Madison, Madison, WI 53706

Corresponding Author: ntambi{at}biochem.wisc.edu

Stearoyl-CoA desaturase (SCD) is an endoplasmic reticulum (ER) protein which catalyzes the delta9-cis desaturation of saturated fatty acids. Mice with targeted disruption in SCD1 (Scd1-/-) have significant reduction in the tissue content of triglycerides, suggesting that monounsaturated fatty acids endogenously synthesized by SCD1 are important for triglyceride synthesis. Acyl-CoA: diacylglycerol acyltransferase (DGAT) is the enzyme which catalyzes the final reaction in the synthesis of triglycerides. The lack of DGAT2, one of the two DGAT isoforms, results in almost a complete loss of tissue triglycerides. We hypothesize that SCD1 participates in triglyceride synthesis by providing a more accessible pool of monounsaturated fatty acids through substrate channeling. In this study, we test whether SCD1 is proximal to DGAT2 by co-localization study with confocal microscopy, co-immunoprecipitation and fluorescence resonance energy transfer (FRET) using HeLa cells as the model of study. All the results suggest that SCD1 and DGAT2 are located very close to each other in the ER, which is a very important criterion for the channeling of substrate. By performing subcellular fractionation using mouse livers, we also show, for the first time, that SCD is present in the mitochondria-associated-membrane (MAM).


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