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Monoacylglycerol O-acyltransferase 1 (MGAT1) localizes to the ER and lipid droplets promoting triacylglycerol synthesis

Authors
 Yoo Jeong Lee  ;  Jae-woo Kim 
Citation
 BMB Reports, Vol.50(7) : 367-372, 2017 
Journal Title
 BMB Reports 
ISSN
 1976-6696 
Issue Date
2017
MeSH
Acyltransferases/metabolism* ; Animals ; COS Cells ; Cells, Cultured ; Cercopithecus aethiops ; Endoplasmic Reticulum/metabolism* ; HEK293 Cells ; Humans ; Lipid Droplets/metabolism* ; Mice ; Triglycerides/biosynthesis*
Keywords
DGAT2 ; Hepatic steatosis ; Lipid droplet ; MGAT1 ; Triacylglycerol synthesis
Abstract
Monoacylglycerol acyltransferase 1 (MGAT) is a microsomal enzyme that catalyzes the synthesis of diacylglycerol (DAG) and triacylglycerol (TAG). However, the subcellular localization and catalytic function domain of this enzyme is poorly understood. In this report, we identified that murine MGAT1 localizes to the endoplasmic reticulum (ER) under normal conditions, whereas MGAT1 co-localize to the lipid droplets (LD) under conditions of enriching fatty acids, contributing to TAG synthesis and LD expansion. For the enzyme activity, both the N-terminal transmembrane domain and catalytic HPHG motif are required. We also show that the transmembrane domain of MGAT1 consists of two hydrophobic regions in the 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 to synergistically increase the TAG biosynthesis and LD expansion, leading to enhancement of lipid accumulation in the liver and fat.
Files in This Item:
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DOI
10.5483/BMBRep.2017.50.7.036
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Biochemistry and Molecular Biology (생화학-분자생물학교실) > 1. Journal Papers
Yonsei Authors
김재우(Kim, Jae Woo) ORCID logo https://orcid.org/0000-0001-5456-9495
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URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/160547
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