GO:0003985 acetyl-CoA C-acetyltransferase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0003985 (acetyl-CoA C-acetyltransferase activity) catalyzes the reversible condensation of two acetyl-CoA molecules into acetoacetyl-CoA and free CoA, a central reaction in ketogenesis, isoprenoid biosynthesis, and mitochondrial fatty acid oxidation.
• The enzyme is encoded by ACAT1 in mitochondria and ACAT2 in the cytosol of eukaryotes, and by orthologs such as EkAACT in plants; these enzymes are also known as acetoacetyl-CoA thiolases.
• ACAT1 supports natural killer cell-dependent antitumor immunity in colorectal cancer, and its loss or inhibition can reshape the tumor immune microenvironment.
• ACAT1-mediated acetylation of ME2 links glutaminolysis to lactate production and drives chemoresistance in ovarian cancer.
• ACAT2 crotonylation downstream of glutaryl-CoA dehydrogenase dysregulates cholesterol metabolism in pancreatic cancer cells, highlighting a role in metabolic reprogramming.
• Modulating cholesterol metabolism through ACAT1 in CD8+ T cells can potentiate antitumor responses, making this activity a candidate immuno-metabolic target.
Description
Acetyl-CoA C-acetyltransferase activity (GO:0003985) is a molecular function that catalyzes the reversible reaction 2 acetyl-CoA = CoA + acetoacetyl-CoA. This thiolase reaction sits at the crossroads of ketone body synthesis, mitochondrial fatty acid oxidation, and the mevalonate pathway for cholesterol and isoprenoid production. Because it controls the flux of acetyl-CoA into acetoacetyl-CoA, the enzyme influences cellular energy homeostasis, membrane biosynthesis, and the availability of substrates for post-translational modifications. Researchers study GO:0003985 to understand how metabolic rewiring supports cancer cell proliferation, immune cell function, and adaptation to nutrient stress. The activity is encoded by distinct genes in different compartments: ACAT1 in mitochondria and ACAT2 in the cytosol, with plant orthologs such as EkAACT providing insight into conserved catalytic mechanisms. Dysregulation of this activity has been linked to tumor immune evasion, chemoresistance, and altered cholesterol metabolism, making it a compelling target for functional genomics and therapeutic development.
acetyl-CoA C-acetyltransferase activity At A Glance
| GO ID | GO:0003985 |
|---|---|
| GO term | acetyl-CoA C-acetyltransferase activity |
| Ontology | molecular_function |
| Synonym | acetoacetyl-CoA thiolase activity; acetyl coenzyme A thiolase activity |
| Major function | Catalysis of the reversible condensation of two acetyl-CoA molecules to acetoacetyl-CoA and CoA |
| Representative genes | ACAT1 (mitochondrial), ACAT2 (cytosolic), EkAACT (plant ortholog) |
| Pathway context | Ketogenesis, fatty acid oxidation, mevalonate/isoprenoid biosynthesis, cholesterol metabolism |
| Disease relevance | Cancer metabolism, immune evasion, chemoresistance, cholesterol-linked immunosuppression |
What Is GO:0003985?
In simple terms, acetyl-CoA C-acetyltransferase activity is the enzyme function that joins two molecules of acetyl-CoA together to form acetoacetyl-CoA and coenzyme A. This is a reversible thiolase reaction that can also run in the opposite direction to break acetoacetyl-CoA down into two acetyl-CoA molecules. The activity is defined by the Gene Ontology as catalysis of the reaction 2 acetyl-CoA = CoA + acetoacetyl-CoA, and it is synonymous with acetoacetyl-CoA thiolase activity and acetyl coenzyme A thiolase activity. It belongs to the molecular_function aspect of GO and is carried out by enzymes such as ACAT1 and ACAT2 in humans and EkAACT in plants.
Why Is acetyl-CoA C-acetyltransferase activity Important in Cell Biology?
GO:0003985 is important because it controls a metabolic branch point that determines whether acetyl-CoA is used for energy production, ketone body synthesis, or cholesterol and isoprenoid biosynthesis. This makes the activity central to how cells adapt to nutrient availability and how tumors rewire metabolism to support growth and immune evasion. In immune cells, ACAT1-dependent cholesterol metabolism influences CD8+ T cell antitumor responses and natural killer cell function, linking this enzymatic activity directly to cancer immunosurveillance. In pancreatic cancer, histone lactylation-driven feedback loops modulate cholesterol-linked immunosuppression, and ACAT2 crotonylation dysregulates cholesterol metabolism, showing that this activity participates in epigenetic and post-translational regulatory networks. Because the reaction is reversible and uses a conserved thiolase mechanism, it is also a tractable target for chemical inhibition and genetic perturbation, making it a high-value node for both mechanistic studies and therapeutic development.
• Controls the reversible conversion of acetyl-CoA to acetoacetyl-CoA, a key step in ketogenesis and isoprenoid biosynthesis.
• Supports natural killer cell-dependent antitumor immunity in colorectal cancer through mitochondrial ACAT1.
• Modulates cholesterol metabolism in CD8+ T cells, with effects on antitumor response.
• Links glutaminolysis to lactate production and chemoresistance in ovarian cancer via ACAT1-mediated ME2 acetylation.
• ACAT2 crotonylation downstream of glutaryl-CoA dehydrogenase dysregulates cholesterol metabolism in pancreatic cancer cells.
• Participates in histone lactylation-driven feedback loops that modulate cholesterol-linked immunosuppression in pancreatic cancer.
• Provides acetyl-CoA-derived acetoacetyl-CoA for the mevalonate pathway, influencing membrane synthesis and protein prenylation.
• Is conserved across plants and animals, enabling comparative studies of thiolase structure and function.
• Represents a potential immuno-metabolic target for modulating tumor microenvironment and immunotherapy response.
• Can be studied with CRISPR knockout, point mutation, and overexpression models to dissect isoform-specific roles.
Molecular Mechanism of acetyl-CoA C-acetyltransferase activity
Substrate binding and acetyl-CoA orientation
In simple terms: The enzyme grabs two acetyl-CoA molecules and positions them so they can react.
Acetyl-CoA C-acetyltransferase binds two molecules of acetyl-CoA in its active site. The enzyme uses a conserved cysteine residue to form a covalent acetyl-enzyme intermediate, releasing the first CoA. The second acetyl-CoA then acts as an acceptor, and the thiolate of the first acetyl group attacks the carbonyl carbon of the second, forming acetoacetyl-CoA and releasing the second CoA. This ping-pong mechanism is characteristic of thiolases and is reversible, allowing the enzyme to catalyze both condensation and cleavage depending on substrate availability.
Catalytic cycle and thiolase fold
In simple terms: A chemical hand-off between two acetyl groups builds acetoacetyl-CoA.
The catalytic cycle proceeds through an acetyl-enzyme thioester intermediate. The active site includes a catalytic triad or dyad with a cysteine nucleophile, a histidine base, and often a second cysteine or glutamate that stabilizes the intermediate. The thiolase fold comprises a five-layered alpha-beta-alpha-beta-alpha structure that forms a tunnel for substrate channeling. This architecture is conserved from bacterial to human enzymes and is shared by ACAT1 and ACAT2, although their subcellular localization and regulation differ.
Cofactors and metal independence
In simple terms: The enzyme does not need metal helpers; it uses its own amino acids to do the chemistry.
Acetyl-CoA C-acetyltransferase activity is metal-independent. It relies on the reactivity of the cysteine thiol and general acid-base catalysis by histidine and other residues. No exogenous cofactors such as NAD+ or FAD are required, distinguishing it from dehydrogenases and oxidoreductases. This simplicity makes the enzyme amenable to kinetic studies and to inhibition by thiol-reactive compounds, which can be used to probe its function in cells.
Regulation by substrate availability and post-translational modification
In simple terms: How much acetyl-CoA is around, and chemical tags on the enzyme, control its speed.
The activity is regulated by the availability of acetyl-CoA, which fluctuates with nutrient status, and by post-translational modifications. In ovarian cancer, ACAT1-mediated acetylation of ME2 links glutaminolysis to lactate production, indicating that ACAT1 can influence other proteins through acetylation. In pancreatic cancer, ACAT2 crotonylation downstream of glutaryl-CoA dehydrogenase dysregulates cholesterol metabolism, showing that lysine acylation can modulate the enzyme or its partners. Histone lactylation-driven feedback loops further connect this activity to cholesterol-linked immunosuppression.
Isoform-specific roles in mitochondria and cytosol
In simple terms: Different versions of the enzyme work in different parts of the cell.
ACAT1 is localized to mitochondria, where it participates in ketogenesis and fatty acid oxidation, while ACAT2 is cytosolic and contributes to the mevalonate pathway for cholesterol synthesis. In colorectal cancer, nuclear mitochondrial ACAT1 orchestrates natural killer cell-dependent antitumor immunity, suggesting non-canonical localization or signaling roles. The distinct compartments allow the same catalytic activity to serve different metabolic fates for acetyl-CoA, and isoform-specific targeting is therefore important for therapeutic strategies.
Key Genes Involved in GO:0003985 acetyl-CoA C-acetyltransferase activity
The following genes encode enzymes with acetyl-CoA C-acetyltransferase activity or directly regulate this activity in human and model systems.
| Gene | Major Role | Research Relevance |
|---|---|---|
| ACAT1 | Mitochondrial acetyl-CoA C-acetyltransferase; catalyzes acetyl-CoA to acetoacetyl-CoA | Supports NK cell antitumor immunity in colorectal cancer; modulates cholesterol metabolism in T cells |
| ACAT2 | Cytosolic acetyl-CoA C-acetyltransferase; contributes to mevalonate pathway | Crotonylation dysregulates cholesterol metabolism in pancreatic cancer |
| ME2 | Malic enzyme 2; acetylated by ACAT1, links glutaminolysis to lactate production | Drives chemoresistance in ovarian cancer |
| GCDH | Glutaryl-CoA dehydrogenase; drives ACAT2 crotonylation | Targeting GCDH dysregulates cholesterol metabolism in pancreatic cancer |
| TREM2 | Microglial receptor regulating cholesterol metabolism | Regulates microglial cholesterol metabolism upon chronic phagocytic challenge |
| EkAACT | Plant acetyl-CoA C-acetyltransferase from Euphorbia kansui | Molecular cloning and analysis of conserved thiolase |
| HMGCR | Rate-limiting enzyme in mevalonate pathway downstream of acetoacetyl-CoA | Cholesterol synthesis context for ACAT activity |
| SQLE | Squalene epoxidase in cholesterol biosynthesis | Cholesterol metabolism modulation in T cells |
| CYP46A1 | Cholesterol 24-hydroxylase | Microglial cholesterol turnover |
| ABCA1 | Cholesterol efflux transporter | Microglial cholesterol metabolism |
| APOE | Cholesterol transport apolipoprotein | Microglial cholesterol metabolism |
| LDHA | Lactate dehydrogenase A; linked to ACAT1-ME2 axis | Lactate production in ovarian cancer chemoresistance |
| GLS | Glutaminase; upstream of glutaminolysis | Links glutaminolysis to ACAT1-mediated ME2 acetylation |
| ACLY | ATP-citrate lyase; generates acetyl-CoA | Provides substrate for ACAT activity |
| ACSS2 | Acetyl-CoA synthetase 2; generates acetyl-CoA from acetate | Substrate supply for ACAT activity |
| SLC25A1 | Mitochondrial citrate carrier | Supports acetyl-CoA production for ACAT1 |
| NAT10 | N-acetyltransferase; ac4C modification | Facilitates TNBC progression and glycolysis addiction |
| JunB | Transcription factor regulated by NAT10/ac4C | Drives glycolysis addiction in TNBC |
How Is acetyl-CoA C-acetyltransferase activity Regulated?
Acetyl-CoA C-acetyltransferase activity is regulated at multiple levels. Substrate availability of acetyl-CoA, which is influenced by glycolysis, fatty acid oxidation, and glutaminolysis, directly controls flux through the reaction. Post-translational modifications such as acetylation and crotonylation modulate the enzyme or its interaction partners; for example, ACAT1-mediated ME2 acetylation links glutaminolysis to lactate production in ovarian cancer, and ACAT2 crotonylation downstream of GCDH dysregulates cholesterol metabolism in pancreatic cancer. Histone lactylation-driven feedback loops further integrate this activity with cholesterol-linked immunosuppression. In immune cells, cholesterol metabolism regulated by ACAT1 affects CD8+ T cell antitumor responses, suggesting that inflammatory signals and metabolic checkpoints converge on this activity. TREM2 signaling in microglia also regulates cholesterol metabolism, providing a neuroimmune context for regulation.
acetyl-CoA C-acetyltransferase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| ACAT1 | Ovarian cancer chemoresistance via ME2 acetylation | ACAT1 knockout ovarian cancer cell lines; point mutation of catalytic cysteine |
| ACAT1 | Colorectal cancer antitumor immunity | ACAT1 knockout colorectal cancer cells; NK cell co-culture |
| ACAT2 | Pancreatic cancer cholesterol metabolism | ACAT2 knockout or crotonylation-site mutant pancreatic cancer cells |
| TREM2 | Microglial cholesterol metabolism in neurodegeneration | TREM2 knockout microglia; phagocytic challenge |
| NAT10 | Triple-negative breast cancer glycolysis addiction | NAT10 knockout TNBC cells; ac4C profiling |
Cancer metabolism and chemoresistance
ACAT1-mediated acetylation of ME2 drives chemoresistance in ovarian cancer by linking glutaminolysis to lactate production, indicating that acetyl-CoA C-acetyltransferase activity can promote a metabolic state that protects tumor cells from chemotherapy. In pancreatic cancer, ACAT2 crotonylation downstream of glutaryl-CoA dehydrogenase dysregulates cholesterol metabolism, and histone lactylation-driven feedback loops modulate cholesterol-linked immunosuppression. These findings position GO:0003985 as a node in tumor metabolic reprogramming and immune evasion.
Antitumor immunity
Nuclear mitochondrial ACAT1 orchestrates natural killer cell-dependent antitumor immunity in colorectal cancer, showing that this enzymatic activity influences immune surveillance. Potentiating the antitumor response of CD8+ T cells by modulating cholesterol metabolism further supports a role for ACAT1 in T cell function. Together, these studies suggest that targeting acetyl-CoA C-acetyltransferase activity could enhance immunotherapy responses.
Neurodegeneration and microglial cholesterol metabolism
TREM2 regulates microglial cholesterol metabolism upon chronic phagocytic challenge, linking cholesterol handling to neurodegenerative disease mechanisms. Because acetyl-CoA C-acetyltransferase activity supplies acetoacetyl-CoA for cholesterol synthesis, its dysfunction could contribute to microglial lipid dysregulation. However, direct evidence for ACAT1 or ACAT2 in neurodegeneration remains an active area of research.
Triple-negative breast cancer and glycolysis addiction
NAT10/ac4C/JunB facilitates TNBC malignant progression and immunosuppression by driving glycolysis addiction, which may intersect with acetyl-CoA metabolism and ACAT activity. Although direct evidence for GO:0003985 in TNBC is limited, the metabolic coupling suggests a potential role that warrants further investigation.
From acetyl-CoA C-acetyltransferase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does ACAT1 catalytic activity suppress tumor growth? | ACAT1 knockout cell line and xenograft |
| How does ACAT1 acetylation of ME2 affect chemoresistance? | ACAT1 point mutant (acetylation-deficient) knock-in ovarian cancer cells |
| What is the role of ACAT2 crotonylation in cholesterol metabolism? | ACAT2 crotonylation-site mutant knock-in pancreatic cancer cells |
| Can ACAT1 overexpression enhance antitumor immunity? | ACAT1 overexpression in CD8+ T cells or NK cells |
| How does TREM2 regulate microglial cholesterol metabolism? | TREM2 knockout microglia with phagocytic challenge |
| Does NAT10-mediated ac4C modification affect glycolysis through ACAT? | NAT10 knockout TNBC cells with metabolic profiling |
How to Study the acetyl-CoA C-acetyltransferase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Spectrophotometric thiolase assay | Enzymatic conversion of acetyl-CoA to acetoacetyl-CoA | Validate ACAT1/ACAT2 knockout or mutant cell lines |
| LC-MS metabolomics | Levels of acetyl-CoA, acetoacetyl-CoA, cholesterol intermediates | Assess metabolic impact of ACAT perturbation |
| 13C stable isotope tracing | Flux through ACAT reaction and downstream pathways | Determine contribution to ketogenesis and lipogenesis |
| Immunoprecipitation and western blot | Acetylation or crotonylation of ACAT and interacting proteins | Study post-translational regulation |
| NK cell cytotoxicity assay | Tumor cell killing by natural killer cells | Evaluate ACAT1 role in antitumor immunity |
| CD8+ T cell activation assay | Cytokine production and proliferation | Test cholesterol metabolism modulation |
| Microglial phagocytosis assay | Cholesterol handling upon phagocytic challenge | Study TREM2-ACAT axis |
| RNA-seq | Transcriptional changes upon ACAT knockout or overexpression | Identify downstream pathways |
Enzymatic activity assays
Direct measurement of acetyl-CoA C-acetyltransferase activity can be performed using spectrophotometric assays that monitor the disappearance of acetyl-CoA or the formation of acetoacetyl-CoA. These assays are essential for validating CRISPR knockout or point mutant models and for determining kinetic parameters such as Km and Vmax.
Metabolic profiling and flux analysis
Metabolic profiling using mass spectrometry can quantify acetyl-CoA, acetoacetyl-CoA, cholesterol intermediates, and lactate. Stable isotope tracing with 13C-acetyl-CoA or 13C-glucose can reveal flux through the ACAT reaction and its contribution to ketogenesis, lipogenesis, and the mevalonate pathway.
Post-translational modification analysis
Acetylation and crotonylation of ACAT1, ACAT2, and interacting proteins such as ME2 can be assessed by immunoprecipitation followed by western blot or mass spectrometry. These methods help dissect how modifications regulate enzymatic activity and downstream signaling.
Immune cell functional assays
Co-culture of tumor cells with natural killer cells or CD8+ T cells, combined with ACAT1 knockout or overexpression, can measure effects on cytotoxicity and cytokine production. These assays link acetyl-CoA C-acetyltransferase activity to antitumor immunity.
How CRISPR Can Be Used to Study GO:0003985 acetyl-CoA C-acetyltransferase activity
Knockout
CRISPR knockout of ACAT1 or ACAT2 can abolish acetyl-CoA C-acetyltransferase activity, allowing researchers to assess its role in cancer cell proliferation, immune evasion, and metabolic reprogramming. Knockout models have been used to show that ACAT1 loss affects natural killer cell-dependent antitumor immunity in colorectal cancer and that ACAT2 loss alters cholesterol metabolism in pancreatic cancer cells.
Point Mutation
Point mutations in the catalytic cysteine or substrate-binding residues of ACAT1 or ACAT2 can separate enzymatic activity from scaffolding functions. Such mutants are valuable for dissecting whether acetylation of ME2 or crotonylation of ACAT2 depends on catalytic activity.
Knock-in
Knock-in of tagged ACAT1 or ACAT2 (e.g., FLAG or HA) enables immunoprecipitation and proteomic identification of interacting partners. Knock-in of acetylation- or crotonylation-site mutants can test the functional relevance of specific post-translational modifications in ovarian and pancreatic cancer models.
Overexpression
Overexpression of ACAT1 or ACAT2 can drive metabolic flux toward acetoacetyl-CoA and cholesterol synthesis, potentially enhancing antitumor immunity or chemoresistance depending on context. Overexpression in CD8+ T cells or NK cells can test whether increasing this activity potentiates immune responses.
How EDITGENE Supports acetyl-CoA C-acetyltransferase activity Research
Researchers studying acetyl-CoA C-acetyltransferase activity-related genes often need to determine whether a candidate gene is causally involved in metabolic reprogramming, immune evasion, or chemoresistance. EDITGENE provides a comprehensive suite of CRISPR-based services to generate precisely engineered cell models that answer these questions.
Contact EDITGENE today to design your custom CRISPR model for acetyl-CoA C-acetyltransferase activity research.
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| ACAT1 Knockout HEK293 Cell Line | EDJ-KQ2122 | Human | 38 | Details Get a Quote |
| HADHA Knockout HEK293 Cell Line | EDJ-KQ2238 | Human | 3030 | Details Get a Quote |
| ACAA1 Knockout HEK293 Cell Line | EDJ-KQ3991 | Human | 30 | Details Get a Quote |
| ACAT2 Knockout HEK293 Cell Line | EDJ-KQ3994 | Human | 39 | Details Get a Quote |
| HADHB Knockout HEK293 Cell Line | EDJ-KQ4838 | Human | 3032 | Details Get a Quote |
| ACAA2 Knockout HEK293 Cell Line | EDJ-KQ7051 | Human | 10449 | Details Get a Quote |
| ACAT1 Knockout A-549 Cell Line | EDJ-KQ22270 | Human | 38 | Details Get a Quote |
| ACAT1 Knockout HCT 116 Cell Line | EDJ-KQ22271 | Human | 38 | Details Get a Quote |
| ACAT1 Knockout HeLa Cell Line | EDJ-KQ22272 | Human | 38 | Details Get a Quote |
| HADHA Knockout A-549 Cell Line | EDJ-KQ22530 | Human | 3030 | Details Get a Quote |
| HADHA Knockout HCT 116 Cell Line | EDJ-KQ22531 | Human | 3030 | Details Get a Quote |
| HADHA Knockout HeLa Cell Line | EDJ-KQ22532 | Human | 3030 | Details Get a Quote |
| ACAA1 Knockout A-549 Cell Line | EDJ-KQ26305 | Human | 30 | Details Get a Quote |
| ACAA1 Knockout HCT 116 Cell Line | EDJ-KQ26306 | Human | 30 | Details Get a Quote |
| ACAA1 Knockout HeLa Cell Line | EDJ-KQ26307 | Human | 30 | Details Get a Quote |
Displaying Records 1 To 15 Of 24 Records
Frequently Asked Questions About acetyl-CoA C-acetyltransferase activity
What is acetyl-CoA C-acetyltransferase activity?
It is the enzymatic activity that catalyzes the reversible conversion of two acetyl-CoA molecules into acetoacetyl-CoA and coenzyme A, encoded by GO:0003985.
What genes encode acetyl-CoA C-acetyltransferase activity?
In humans, ACAT1 encodes the mitochondrial enzyme and ACAT2 encodes the cytosolic enzyme; plant orthologs include EkAACT.
What is the role of ACAT1 in cancer?
ACAT1 supports natural killer cell-dependent antitumor immunity in colorectal cancer and mediates ME2 acetylation that drives chemoresistance in ovarian cancer.
How is acetyl-CoA C-acetyltransferase activity regulated?
It is regulated by acetyl-CoA availability and by post-translational modifications such as acetylation and crotonylation, which can affect enzyme function and downstream metabolism.
What diseases are associated with ACAT1 and ACAT2?
They are associated with cancer chemoresistance, cholesterol metabolism disorders, and immune evasion, with emerging links to neurodegeneration through microglial cholesterol handling.
How can I study acetyl-CoA C-acetyltransferase activity in the lab?
You can use enzymatic assays, metabolomics, and CRISPR knockout or point mutation models to measure activity and downstream effects.
What is the difference between ACAT1 and ACAT2?
ACAT1 is mitochondrial and involved in ketogenesis and fatty acid oxidation, while ACAT2 is cytosolic and contributes to cholesterol synthesis via the mevalonate pathway.
Can acetyl-CoA C-acetyltransferase activity be targeted therapeutically?
Yes, it is considered a potential immuno-metabolic target, and modulating cholesterol metabolism through ACAT1 can potentiate antitumor responses.
What CRISPR models are available for ACAT1 research?
Knockout, point mutation, knock-in, and overexpression models can be generated to dissect catalytic and non-catalytic functions.
How does ACAT2 crotonylation affect pancreatic cancer?
ACAT2 crotonylation downstream of glutaryl-CoA dehydrogenase dysregulates cholesterol metabolism in pancreatic cancer cells.
Conclusion
Acetyl-CoA C-acetyltransferase activity (GO:0003985) is a fundamental metabolic function that bridges acetyl-CoA utilization with ketogenesis, cholesterol synthesis, and immune regulation. Its roles in cancer chemoresistance, antitumor immunity, and microglial cholesterol metabolism make it a high-priority target for mechanistic and translational research. By leveraging CRISPR knockout, point mutation, knock-in, and overexpression models, researchers can dissect the isoform-specific and context-dependent functions of ACAT1 and ACAT2. EDITGENE provides end-to-end services to accelerate these discoveries and support the development of novel therapeutic strategies.
References
- 1. Yang J et al.. 2025. Histone lactylation-driven feedback loop modulates cholesterol-linked immunosuppression in pancreatic cancer.. Gut 74(11):1859-1872 PMID: 40467104
- 2. Wei C et al.. 2025. Nuclear mitochondrial acetyl-CoA acetyltransferase 1 orchestrates natural killer cell-dependent antitumor immunity in colorectal cancer.. Signal Transduct Target Ther 10(1):138 PMID: 40289129
- 3. Nugent AA et al.. 2020. TREM2 Regulates Microglial Cholesterol Metabolism upon Chronic Phagocytic Challenge.. Neuron 105(5):837-854.e9 PMID: 31902528
- 4. Yang W et al.. 2016. Potentiating the antitumour response of CD8(+) T cells by modulating cholesterol metabolism.. Nature 531(7596):651-5 PMID: 26982734
- 5. Zheng C et al.. 2025. ACAT1-Mediated ME2 Acetylation Drives Chemoresistance in Ovarian Cancer by Linking Glutaminolysis to Lactate Production.. Adv Sci (Weinh) 12(14):e2416467 PMID: 39951294
- 6. Li G et al.. 2024. NAT10/ac4C/JunB facilitates TNBC malignant progression and immunosuppression by driving glycolysis addiction.. J Exp Clin Cancer Res 43(1):278 PMID: 39363363
- 7. Wang M et al.. 2022. Molecular Cloning and Analysis of an Acetyl-CoA C-acetyltransferase Gene (EkAACT) from Euphorbia kansui Liou.. Plants (Basel) 11(12) PMID: 35736690
- 8. Han F et al.. 2026. Targeting glutaryl-CoA dehydrogenase-driven acetyl coenzyme A acetyltransferase 2 crotonylation dysregulates cholesterol metabolism in pancreatic cancer cells.. Int J Biol Macromol 335(Pt 2):149182 PMID: 41285334
