ArticleBMB reports2017
Monoacylglycerol O-acyltransferase 1 (MGAT1) localizes to the ER and lipid droplets promoting triacylglycerol synthesis.
Article in BMB reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
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- Active Glycogen Synthase in the Liver Prevents High-Fat Diet-Induced Glucose Intolerance, Decreases Food Intake, and Lowers Body Weight.International journal of molecular sciences · 2023Article
- Transmembrane Protein 68 Functions as an MGAT and DGAT Enzyme for Triacylglycerol Biosynthesis.International journal of molecular sciences · 2023Article
- Assessment of the association of the MOGAT1 and MOGAT3 gene with growth traits in different growth stages in Holstein calves.Archives animal breeding · 2022Article
- Lipid metabolism is altered in maternal, placental, and fetal tissues of ewes with small for gestational age fetuses†.Biology of reproduction · 2021Article
- Step-by-Step Construction of Gene Co-Expression Network Analysis for Identifying Novel Biomarkers of Sepsis Occurrence and Progression.International journal of general medicine · 2021Article
- Xanthohumol ameliorates Diet-Induced Liver Dysfunction via Farnesoid X Receptor-Dependent and Independent Signaling.Frontiers in pharmacology · 2021Article
- Under-carboxylated osteocalcin regulates glucose and lipid metabolism during pregnancy and lactation in rats.Journal of endocrinological investigation · 2020Article
- OSBP-related protein-2 (ORP2): a novel Akt effector that controls cellular energy metabolism.Cellular and molecular life sciences : CMLS · 2018Article
- Association between theInternational journal of clinical and experimental pathology · 2018Article
- Beef, Casein, and Soy Proteins Differentially Affect Lipid Metabolism, Triglycerides Accumulation and Gut Microbiota of High-Fat Diet-Fed C57BL/6J Mice.Frontiers in microbiology · 2018Article
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2 authors at 2 institutions in 1 country.
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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. [BMB Reports 2017; 50(7): 367-372].
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