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This galley proof is being listed electronically before publishing the final manuscript (It's not final version).

Monoacylglycerol O-acyltransferase 1 (MGAT1) localizes to the ER and lipid droplets promoting triacylglycerol synthesis
Yoo Jeong Lee1, Jae-woo Kim2,*
1Division of Metabolic Disease, National Institutes of Health, Korea,
2Dept Biochem and Mol Biol, Yonsei University College of Medicine
Monoacylglycerol acyltransferase 1 (MGAT) was identified as a microsomal enzyme that catalyzes the synthesis of diacylglycerol (DAG) and triacylglycerol (TAG), but the subcellular localization and catalytic function domain of this enzyme is poorly understood. In this report, we identify that murine MGAT1 localizes to the endoplasmic reticulum (ER) with basal condition, whereas, under conditions of enriching fatty acids, MGAT1 also co-localize to the lipid droplets (LD), contributing TAG synthesis and LD expansion. For the enzyme activity, both N-terminal transmembrane domain and catalytic HPHG motif are required. We also show that transmembrane domain of MGAT1 consists of two hydrophobic regions in N-terminus, and the consensus sequence FLXLXXXn, a putative neutral lipid-binding domain, exists in the first transmembrane domain. Finally, MGAT1 interacts with DGAT2, which serves synergistic increase in TAG biosynthesis and LD expansion, leading to enhance of lipid accumulation in liver and fat.
Abstract, Accepted Manuscript(in press) [Submitted on March 6, 2017, Accepted on March 22, 2017]
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