GO:0016411 acylglycerol O-acyltransferase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0016411 acylglycerol O-acyltransferase activity describes the catalysis of acyl group transfer to an oxygen atom on an acylglycerol molecule, a central reaction in triacylglycerol synthesis.
• The terminal and rate-limiting step of triacylglycerol biosynthesis is catalyzed by diacylglycerol O-acyltransferase (DGAT) enzymes, which convert diacylglycerol to triacylglycerol using acyl-CoA as the acyl donor.
• DGAT1 is a membrane-embedded enzyme whose structure and catalytic mechanism have been resolved, revealing a conserved acyltransferase fold and a tunnel for substrate access.
• PNPLA3-I148M is a gain-of-function neomorph that interferes with hepatic triglyceride clearance and promotes steatosis, highlighting the pathophysiological importance of acylglycerol O-acyltransferase activity.
• Glycerol kinase drives hepatic de novo lipogenesis and triglyceride synthesis by activating SREBP-1c and upregulating DGAT1/2 expression, linking acylglycerol O-acyltransferase activity to nonalcoholic fatty liver disease.
• CHP1 promotes lipid droplet growth and regulates the localization of key enzymes for triacylglycerol synthesis, providing a spatial regulatory layer for acylglycerol O-acyltransferase activity.
Description
Acylglycerol O-acyltransferase activity (GO:0016411) is a molecular function defined as the catalysis of acyl group transfer to an oxygen atom on an acylglycerol molecule. This activity is essential for the biosynthesis of triacylglycerols (TAGs), the major form of stored energy in eukaryotes, and for the remodeling of glycerolipid species. The reaction typically uses acyl-CoA as the acyl donor and an acylglycerol such as diacylglycerol as the acceptor, producing triacylglycerol and CoA. Because TAG synthesis is central to lipid homeostasis, the enzymes that carry this activity are intensely studied in metabolic disease, hepatology, and lipid droplet biology. The best-characterized enzymes with acylglycerol O-acyltransferase activity are the diacylglycerol O-acyltransferases DGAT1 and DGAT2, which catalyze the final committed step of TAG synthesis. DGAT1 belongs to the membrane-bound O-acyltransferase (MBOAT) family and has been structurally resolved, revealing how it binds diacylglycerol and acyl-CoA and how it positions them for catalysis. Beyond DGATs, other enzymes such as PNPLA3 can influence TAG hydrolysis and lipid droplet remodeling, and mutations in PNPLA3 are among the strongest genetic determinants of hepatic steatosis. For researchers, GO:0016411 provides a precise functional annotation for genes and proteins involved in glycerolipid metabolism. It is used in genome-wide functional enrichment, CRISPR screen analysis, and pathway modeling of lipid disorders. Understanding the catalytic mechanism, regulation, and disease relevance of acylglycerol O-acyltransferase activity is therefore critical for developing therapeutic strategies against fatty liver disease, obesity, and related metabolic syndromes.
acylglycerol O-acyltransferase activity At A Glance
| GO ID | GO:0016411 |
|---|---|
| GO term | acylglycerol O-acyltransferase activity |
| Ontology | molecular_function |
| Synonym | none |
| Major function | Catalysis of acyl group transfer to an oxygen atom on an acylglycerol molecule, typically producing triacylglycerol from diacylglycerol and acyl-CoA |
| Representative enzymes | DGAT1, DGAT2, and related MBOAT family members |
| Substrates | Acylglycerols (e.g., diacylglycerol) and acyl-CoA |
| Products | Triacylglycerol and CoA |
| Cellular context | Endoplasmic reticulum membrane and lipid droplets |
What Is GO:0016411?
In simple terms, acylglycerol O-acyltransferase activity is the enzyme function that attaches a fatty acid (acyl group) to a glycerol backbone molecule that already contains at least one fatty acid, using an oxygen atom on the acylglycerol as the acceptor. The official QuickGO definition states: Catalysis of the transfer of an acyl group to an oxygen atom on the acylglycerol molecule. This activity is responsible for the final step in triacylglycerol synthesis, where diacylglycerol is converted to triacylglycerol, and it is also involved in the synthesis and remodeling of other acylglycerols.
Why Is acylglycerol O-acyltransferase activity Important in Cell Biology?
Acylglycerol O-acyltransferase activity is important because it catalyzes the terminal and rate-limiting step of triacylglycerol synthesis, directly controlling the storage of excess energy as fat. Dysregulation of this activity contributes to hepatic steatosis, insulin resistance, and dyslipidemia, as shown by genetic and pharmacological studies of DGAT enzymes and PNPLA3. The structural resolution of human DGAT1 has provided a mechanistic framework for designing inhibitors and for understanding how mutations alter catalytic efficiency. Moreover, this activity is spatially and temporally regulated at lipid droplets, where CHP1 and other factors coordinate the localization of TAG-synthesizing enzymes. Consequently, GO:0016411 is a key annotation for metabolic research and drug discovery.
• Catalyzes the final step of triacylglycerol synthesis, a central pathway for energy storage.
• DGAT1 and DGAT2 are therapeutic targets for obesity, diabetes, and nonalcoholic fatty liver disease.
• PNPLA3-I148M, a common variant, promotes hepatic steatosis by interfering with triglyceride hydrolysis, indirectly affecting acylglycerol O-acyltransferase activity.
• Glycerol kinase activation upregulates DGAT1/2 expression and drives de novo lipogenesis in NAFLD.
• CHP1 regulates lipid droplet growth and the localization of key enzymes for triacylglycerol synthesis.
• The activity is essential for lipid droplet biogenesis and maintenance, which are linked to cellular stress responses.
• Moderate exercise alleviates NAFLD by regulating lipid droplet biogenesis and autophagy, processes that intersect with TAG synthesis.
• Gut microbiota can influence hepatic ketogenesis and lipid accumulation, indirectly affecting glycerolipid metabolism.
• Acylglycerol O-acyltransferase activity is a functional annotation used in CRISPR screens and pathway enrichment for metabolic genes.
• Structural knowledge of DGAT1 enables rational design of small-molecule modulators.
Mechanism, Genes and Research Methods
Substrate Binding and Acyl Transfer
In simple terms: The enzyme grabs a fatty acid and a glycerol backbone, then attaches the fatty acid to the glycerol.
Acylglycerol O-acyltransferase activity proceeds through an ordered mechanism in which the enzyme binds an acylglycerol acceptor, such as diacylglycerol, and an acyl-CoA donor. Structural studies of human DGAT1 reveal a conserved MBOAT fold with a membrane-embedded active site that positions the hydroxyl oxygen of diacylglycerol for nucleophilic attack on the thioester carbonyl of acyl-CoA. The reaction releases CoA and forms a new ester bond, yielding triacylglycerol. This catalytic step is the terminal and rate-limiting reaction in the Kennedy pathway of TAG synthesis.
Enzyme Families and Isoforms
In simple terms: Different enzymes can do this job, and they are not all the same.
The principal enzymes with acylglycerol O-acyltransferase activity are DGAT1 and DGAT2. DGAT1 belongs to the membrane-bound O-acyltransferase (MBOAT) family and is widely expressed in tissues, while DGAT2 is a member of the DGAT2 family and is more specialized for lipid storage. Both catalyze the conversion of diacylglycerol to triacylglycerol, but they differ in substrate specificity, tissue distribution, and regulation. Other enzymes, such as PNPLA3, can influence the balance between TAG synthesis and hydrolysis, although PNPLA3 itself is primarily a lipase.
Membrane Topology and Lipid Droplet Association
In simple terms: These enzymes work at membranes and on the surface of fat droplets.
DGAT1 and DGAT2 are integral membrane proteins localized to the endoplasmic reticulum, where they access diacylglycerol and acyl-CoA from the membrane bilayer. As lipid droplets form, TAG-synthesizing enzymes can associate with the droplet surface. CHP1 has been shown to promote lipid droplet growth and to regulate the localization of key enzymes for triacylglycerol synthesis, suggesting that acylglycerol O-acyltransferase activity is spatially organized at droplet-membrane contact sites. This spatial regulation ensures efficient channeling of substrates and products.
Regulation by Transcriptional and Metabolic Signals
In simple terms: The cell can make more or less of these enzymes depending on its needs.
Expression of DGAT1 and DGAT2 is transcriptionally regulated by lipogenic factors. Glycerol kinase drives hepatic de novo lipogenesis and triglyceride synthesis by activating SREBP-1c transcription and upregulating DGAT1/2 expression, linking acylglycerol O-acyltransferase activity to glycerol metabolism. The integrated stress response can also regulate central carbon metabolism and lipid droplet biogenesis, indirectly affecting TAG synthesis. Additionally, gut microbiota can influence hepatic ketogenesis and lipid accumulation, which may alter the demand for acylglycerol O-acyltransferase activity.
Pathophysiological Consequences of Dysregulation
In simple terms: When this activity goes wrong, fat can build up in the liver and cause disease.
Dysregulated acylglycerol O-acyltransferase activity contributes to hepatic steatosis and nonalcoholic fatty liver disease. The PNPLA3-I148M variant is a gain-of-function mutation that promotes steatosis by inhibiting ATGL-mediated triglyceride hydrolysis, leading to increased TAG accumulation. PNPLA3-I148M also acts as a neomorph that interferes with two primary hepatic triglyceride clearance pathways. These findings highlight how altered glycerolipid metabolism, including acylglycerol O-acyltransferase activity, can drive disease. Moderate exercise can alleviate NAFLD by regulating lipid droplet biogenesis and autophagy, offering a lifestyle intervention that intersects with this pathway.
Key Genes Involved in GO:0016411 acylglycerol O-acyltransferase activity
The following genes encode enzymes or regulators that directly or indirectly influence acylglycerol O-acyltransferase activity and triacylglycerol synthesis.
| Gene | Major Role | Research Relevance |
|---|---|---|
| DGAT1 | Catalyzes the final step of triacylglycerol synthesis using diacylglycerol and acyl-CoA | Structural studies and inhibitor development for obesity and NAFLD |
| DGAT2 | Catalyzes diacylglycerol acylation, specialized for lipid storage | Target for hepatic steatosis and insulin resistance |
| PNPLA3 | Lipase that hydrolyzes triglycerides; I148M variant promotes steatosis | Strong genetic risk factor for NAFLD and liver disease |
| GK | Glycerol kinase activates SREBP-1c and upregulates DGAT1/2 | Links glycerol metabolism to de novo lipogenesis in NAFLD |
| SREBP-1c | Transcription factor that upregulates lipogenic genes including DGAT1/2 | Master regulator of hepatic lipogenesis |
| CHP1 | Promotes lipid droplet growth and regulates localization of TAG synthesis enzymes | Spatial regulator of acylglycerol O-acyltransferase activity |
| ATGL | Triglyceride lipase; inhibited by PNPLA3-I148M | Key enzyme in triglyceride hydrolysis and lipid droplet turnover |
| MBOAT family | Family of membrane-bound O-acyltransferases including DGAT1 | Provides structural and mechanistic framework |
| DGAT2 family | Family of diacylglycerol acyltransferases | Alternative TAG synthesis pathway |
| SREBP-1 | Lipogenic transcription factor | Regulates DGAT1/2 expression |
| Glycerol kinase | Phosphorylates glycerol, feeding into lipogenesis | Connects glycerol metabolism to TAG synthesis |
| PNPLA3-I148M | Gain-of-function neomorph interfering with triglyceride clearance | Model for studying steatosis mechanisms |
| CHP1 | Regulates lipid droplet growth | Potential target for modulating lipid storage |
| ATGL | Adipose triglyceride lipase | Therapeutic target for lipid disorders |
| DGAT1 | Membrane-bound O-acyltransferase | Structural template for drug design |
| DGAT2 | Diacylglycerol acyltransferase | Metabolic engineering target |
| SREBP-1c | Lipogenic transcription factor | Regulates de novo lipogenesis |
| GK | Glycerol kinase | Links glycerol metabolism to TAG synthesis |
How Is acylglycerol O-acyltransferase activity Regulated?
Acylglycerol O-acyltransferase activity is regulated at multiple levels. Transcriptionally, the lipogenic transcription factor SREBP-1c upregulates DGAT1 and DGAT2 expression in response to glycerol kinase activation, linking glycerol metabolism to de novo lipogenesis. The integrated stress response can modulate central carbon metabolism and lipid droplet biogenesis, indirectly affecting TAG synthesis. Post-translationally, the localization of TAG-synthesizing enzymes to lipid droplets is regulated by proteins such as CHP1, which promotes lipid droplet growth and regulates the localization of key enzymes for triacylglycerol synthesis. Additionally, gut microbiota can influence hepatic ketogenesis and lipid accumulation, potentially altering the demand for acylglycerol O-acyltransferase activity. These regulatory layers ensure that TAG synthesis is matched to cellular energy status and metabolic needs.
acylglycerol O-acyltransferase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| PNPLA3 | Nonalcoholic fatty liver disease, hepatic steatosis | Knock-in mouse expressing PNPLA3-I148M; human hepatocyte cell lines |
| DGAT1 | Obesity, insulin resistance, NAFLD | DGAT1 knockout and point-mutation models; structural studies |
| DGAT2 | Hepatic steatosis, dyslipidemia | Liver-specific DGAT2 knockout; overexpression models |
| GK | NAFLD, de novo lipogenesis | Glycerol kinase knockout and overexpression in hepatocytes |
| CHP1 | Lipid droplet growth, metabolic stress | CHP1 knockout and tagged knock-in for localization studies |
Nonalcoholic Fatty Liver Disease (NAFLD)
NAFLD is characterized by excessive hepatic triglyceride accumulation, and acylglycerol O-acyltransferase activity directly contributes to this process. Glycerol kinase drives hepatic de novo lipogenesis and triglyceride synthesis by activating SREBP-1c and upregulating DGAT1/2 expression. The PNPLA3-I148M variant promotes steatosis by inhibiting ATGL-mediated triglyceride hydrolysis, leading to increased TAG accumulation. PNPLA3-I148M also interferes with hepatic triglyceride clearance pathways, further exacerbating lipid storage. Moderate treadmill exercise alleviates NAFLD by regulating lipid droplet biogenesis and autophagy, highlighting the dynamic nature of this pathway.
Metabolic Syndrome and Insulin Resistance
Dysregulated acylglycerol O-acyltransferase activity contributes to ectopic lipid accumulation in liver and muscle, which is associated with insulin resistance. DGAT1 and DGAT2 are key enzymes in this process, and their expression is upregulated by lipogenic signals such as SREBP-1c. The structural resolution of human DGAT1 provides a basis for designing inhibitors that could reduce TAG synthesis and improve metabolic parameters. However, the precise role of individual DGAT isoforms in insulin sensitivity remains an active area of research.
Lipid Droplet Biology and Cellular Stress
Lipid droplets are dynamic organelles that store neutral lipids, and acylglycerol O-acyltransferase activity is essential for their biogenesis and growth. CHP1 promotes lipid droplet growth and regulates the localization of key enzymes for triacylglycerol synthesis. The integrated stress response can regulate central carbon metabolism and lipid droplet biogenesis, linking acylglycerol O-acyltransferase activity to cellular stress adaptation. These connections have implications for understanding how cells cope with metabolic stress and for developing therapies that target lipid droplet dynamics.
From acylglycerol O-acyltransferase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of DGAT1 reduce hepatic triglyceride accumulation? | DGAT1 knockout cell lines and mouse models |
| How does PNPLA3-I148M alter triglyceride hydrolysis? | Knock-in of PNPLA3-I148M in hepatocyte cell lines |
| Does glycerol kinase regulate DGAT1/2 expression? | GK overexpression and knockout in liver cells |
| How does CHP1 regulate lipid droplet growth? | CHP1 knockout and tagged knock-in for imaging |
| Can exercise modulate lipid droplet biogenesis? | Moderate treadmill exercise in NAFLD models |
| Does the integrated stress response affect TAG synthesis? | ISR activation models with lipid droplet analysis |
How to Study the acylglycerol O-acyltransferase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Radiolabeled acyl-CoA assay | Enzymatic conversion of diacylglycerol to triacylglycerol | Quantifying acylglycerol O-acyltransferase activity in vitro |
| Lipidomics (LC-MS) | Glycerolipid species profiles | Assessing changes in TAG and DAG levels |
| X-ray crystallography | Three-dimensional structure of DGAT1 | Mechanistic studies and inhibitor design |
| Fluorescence microscopy | Lipid droplet size and number | Visualizing lipid droplet dynamics |
| Western blotting | Protein expression of DGAT1/2, CHP1 | Validating genetic manipulations |
| qRT-PCR | mRNA levels of lipogenic genes | Measuring transcriptional regulation |
| CRISPR screening | Functional gene identification | Discovering novel regulators of TAG synthesis |
| Co-immunoprecipitation | Protein-protein interactions | Identifying enzyme complexes at lipid droplets |
Enzymatic Activity Assays
Acylglycerol O-acyltransferase activity can be measured using radiolabeled acyl-CoA or fluorescent substrates, followed by lipid extraction and thin-layer chromatography or mass spectrometry. These assays are used to quantify the conversion of diacylglycerol to triacylglycerol in cell lysates or membrane fractions. They are essential for validating enzyme function and for screening inhibitors.
Structural Biology and Modeling
X-ray crystallography and cryo-electron microscopy have been used to determine the structure of human DGAT1, revealing the MBOAT fold and substrate-binding pockets. Structural studies provide mechanistic insights into catalysis and guide the design of small-molecule modulators. Homology modeling can extend these findings to related enzymes.
Lipidomics and Mass Spectrometry
Mass spectrometry-based lipidomics allows comprehensive profiling of glycerolipid species in cells and tissues. This method can quantify changes in triacylglycerol and diacylglycerol levels upon genetic or pharmacological manipulation of acylglycerol O-acyltransferase activity. It is widely used in metabolic disease research.
Imaging and Lipid Droplet Analysis
Fluorescence microscopy with lipid droplet dyes (e.g., BODIPY) enables visualization of lipid droplet number, size, and distribution. Live-cell imaging can track the localization of tagged enzymes such as DGAT1 or CHP1. These methods are critical for understanding spatial regulation of TAG synthesis.
How CRISPR Can Be Used to Study GO:0016411 acylglycerol O-acyltransferase activity
Knockout
CRISPR knockout of DGAT1, DGAT2, or CHP1 can be used to eliminate acylglycerol O-acyltransferase activity and assess its contribution to triglyceride synthesis and lipid droplet formation. Knockout cell lines are valuable for metabolic studies and drug target validation.
Point Mutation
Point mutations such as PNPLA3-I148M can be introduced using CRISPR base editing or homology-directed repair to model human disease variants. These models help dissect how specific mutations alter triglyceride hydrolysis and hepatic steatosis.
Knock-in
Knock-in of tagged versions of DGAT1 or CHP1 (e.g., GFP or HA tags) allows visualization and immunoprecipitation of endogenous proteins. This approach is useful for studying localization and interactors of acylglycerol O-acyltransferase enzymes.
Overexpression
CRISPR activation (CRISPRa) or lentiviral overexpression can increase expression of DGAT1, DGAT2, or glycerol kinase to study the effects of enhanced acylglycerol O-acyltransferase activity on lipid accumulation and cellular metabolism.
How EDITGENE Supports acylglycerol O-acyltransferase activity Research
Researchers studying acylglycerol O-acyltransferase activity-related genes often need to determine whether a candidate gene is causally involved in triglyceride synthesis, lipid droplet biology, or metabolic disease. EDITGENE provides a comprehensive suite of CRISPR-based services to generate precisely engineered cell models for such investigations.
Contact EDITGENE today to design your custom CRISPR model for acylglycerol O-acyltransferase activity research.
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| PNPLA2 Knockout HEK293 Cell Line | EDJ-KQ3484 | Human | 57104 | Details Get a Quote |
| PNPLA4 Knockout HEK293 Cell Line | EDJ-KQ6184 | Human | 8228 | Details Get a Quote |
| PLA2G15 Knockout HEK293 Cell Line | EDJ-KQ8113 | Human | 23659 | Details Get a Quote |
| PNPLA3 Knockout HEK293 Cell Line | EDJ-KQ14822 | Human | 80339 | Details Get a Quote |
| PNPLA4 Knockout A-549 Cell Line | EDJ-KQ30013 | Human | 8228 | Details Get a Quote |
| PNPLA4 Knockout HeLa Cell Line | EDJ-KQ30015 | Human | 8228 | Details Get a Quote |
| PLA2G15 Knockout A-549 Cell Line | EDJ-KQ33992 | Human | 23659 | Details Get a Quote |
| PLA2G15 Knockout HCT 116 Cell Line | EDJ-KQ33993 | Human | 23659 | Details Get a Quote |
| PLA2G15 Knockout HeLa Cell Line | EDJ-KQ33994 | Human | 23659 | Details Get a Quote |
| PNPLA2 Knockout A-549 Cell Line | EDJ-KQ25260 | Human | 57104 | Details Get a Quote |
| PNPLA2 Knockout HCT 116 Cell Line | EDJ-KQ25261 | Human | 57104 | Details Get a Quote |
| PNPLA2 Knockout HeLa Cell Line | EDJ-KQ25262 | Human | 57104 | Details Get a Quote |
| PNPLA4 Knockout HCT 116 Cell Line | EDJ-KQ28706 | Human | 8228 | Details Get a Quote |
| PNPLA3 Knockout A-549 Cell Line | EDJ-KQ45254 | Human | 80339 | Details Get a Quote |
| PNPLA3 Knockout HCT 116 Cell Line | EDJ-KQ45255 | Human | 80339 | Details Get a Quote |
Displaying Records 1 To 15 Of 18 Records
Frequently Asked Questions About acylglycerol O-acyltransferase activity
What is acylglycerol O-acyltransferase activity?
Acylglycerol O-acyltransferase activity (GO:0016411) is the catalysis of acyl group transfer to an oxygen atom on an acylglycerol molecule, typically producing triacylglycerol from diacylglycerol and acyl-CoA.
What genes are involved in acylglycerol O-acyltransferase activity?
Key genes include DGAT1 and DGAT2, which encode the main enzymes catalyzing this reaction, as well as regulators such as PNPLA3, glycerol kinase, and CHP1.
What is the role of DGAT1 in triacylglycerol synthesis?
DGAT1 catalyzes the final step of triacylglycerol synthesis by transferring an acyl group from acyl-CoA to diacylglycerol, and its structure has been resolved to reveal the catalytic mechanism.
How is acylglycerol O-acyltransferase activity regulated?
It is regulated transcriptionally by SREBP-1c, spatially by lipid droplet proteins such as CHP1, and metabolically by glycerol kinase and the integrated stress response.
What diseases are associated with acylglycerol O-acyltransferase activity?
Dysregulation is linked to nonalcoholic fatty liver disease, hepatic steatosis, obesity, and insulin resistance, with PNPLA3-I148M being a strong genetic risk factor.
How can I measure acylglycerol O-acyltransferase activity?
Enzymatic assays using radiolabeled acyl-CoA, lipidomics by mass spectrometry, and fluorescence microscopy of lipid droplets are common methods.
What is the PNPLA3-I148M mutation?
PNPLA3-I148M is a gain-of-function mutation that promotes hepatic steatosis by inhibiting ATGL-mediated triglyceride hydrolysis and interfering with triglyceride clearance.
Can CRISPR be used to study acylglycerol O-acyltransferase activity?
Yes, CRISPR knockout, point mutation, knock-in, and overexpression models can be used to dissect the function of DGAT1, DGAT2, PNPLA3, and other related genes.
What is the difference between DGAT1 and DGAT2?
DGAT1 is a member of the MBOAT family with a resolved structure, while DGAT2 belongs to a distinct family; both catalyze diacylglycerol acylation but differ in tissue distribution and regulation.
How does CHP1 regulate lipid droplets?
CHP1 promotes lipid droplet growth and regulates the localization of key enzymes for triacylglycerol synthesis, thereby influencing acylglycerol O-acyltransferase activity.
Conclusion
Acylglycerol O-acyltransferase activity (GO:0016411) is a fundamental molecular function in glycerolipid metabolism, catalyzing the terminal step of triacylglycerol synthesis. Its dysregulation is intimately linked to hepatic steatosis, NAFLD, and metabolic syndrome, as evidenced by genetic and structural studies of DGAT1, DGAT2, and PNPLA3. Understanding the regulation and spatial organization of this activity, including the roles of CHP1 and glycerol kinase, offers opportunities for therapeutic intervention. For researchers, precise CRISPR models are essential to dissect the causal roles of genes involved in acylglycerol O-acyltransferase activity. EDITGENE provides knockout, point-mutation, knock-in, overexpression, and screening services to accelerate discovery in this field.
References
- 1. Wang Y et al.. 2025. PNPLA3(148M) is a gain-of-function mutation that promotes hepatic steatosis by inhibiting ATGL-mediated triglyceride hydrolysis.. J Hepatol 82(5):871-881 PMID: 39550037
- 2. Ouyang S et al.. 2024. Glycerol Kinase Drives Hepatic de novo Lipogenesis and Triglyceride Synthesis in Nonalcoholic Fatty Liver by Activating SREBP-1c Transcription, Upregulating DGAT1/2 Expression, and Promoting Glycerol Metabolism.. Adv Sci (Weinh) 11(46):e2401311 PMID: 39418169
- 3. Luo Z et al.. 2025. Gut microbiota regulates hepatic ketogenesis and lipid accumulation in ketogenic diet-induced hyperketonemia by disrupting bile acid metabolism.. Gut Microbes 17(1):2496437 PMID: 40268803
- 4. Sherman DJ et al.. 2025. PNPLA3-I148M is a neomorph that interferes with two primary hepatic triglyceride clearance pathways.. Cell Rep 44(10):116371 PMID: 41046517
- 5. Labbé K et al.. 2024. Specific activation of the integrated stress response uncovers regulation of central carbon metabolism and lipid droplet biogenesis.. Nat Commun 15(1):8301 PMID: 39333061
- 6. Yang Y et al.. 2022. Moderate Treadmill Exercise Alleviates NAFLD by Regulating the Biogenesis and Autophagy of Lipid Droplet.. Nutrients 14(22) PMID: 36432597
- 7. Yang G et al.. 2025. CHP1 promotes lipid droplet growth and regulates the localization of key enzymes for triacylglycerol synthesis.. Proc Natl Acad Sci U S A 122(35):e2508912122 PMID: 40875810
- 8. Wang L et al.. 2020. Structure and mechanism of human diacylglycerol O-acyltransferase 1.. Nature 581(7808):329-332 PMID: 32433610
