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- Table of Contents
Facts about 1-acyl-sn-glycerol-3-phosphate acyltransferase beta.
Human | |
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Gene Name: | AGPAT2 |
Uniprot: | O15120 |
Entrez: | 10555 |
Belongs to: |
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1-acyl-sn-glycerol-3-phosphate acyltransferase family |
1-acylglycerol-3-phosphate O-acyltransferase 2 (lysophosphatidic acidacyltransferase, beta); 1-acylglycerol-3-phosphate O-acyltransferase 2; 1-AGPAT 2,1-acylglycerol-3-phosphate O-acyltransferase 2 (lysophosphatidic acidacyltransferase-beta); 1-AGPAT2,1-AGP acyltransferase 2,1-acyl-sn-glycerol-3-phosphate acyltransferase beta; Berardinelli-Seip congenital lipodystrophy; BSCL; BSCL1; EC 2.3.1.51; LPAAB; LPAAT-beta; Lysophosphatidic acid acyltransferase beta; lysophosphatidic acid acyltransferase-beta
Mass (kDA):
30.914 kDA
Human | |
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Location: | 9q34.3 |
Sequence: | 9; NC_000009.12 (136673143..136687457, complement) |
Expressed predominantly in adipose tissue, pancreas and liver.
Endoplasmic reticulum membrane; Multi-pass membrane protein.
When searching for an AGPAT2 mark, you should first ask the following questions: Molecular Functions, Targets, and Other Questions. These are the most important uses of this biomarker as well as their respective molecular function. We will also discuss the regulatory mechanisms of this marker and the targets of the gene. After this, you can proceed to the next section where we will cover the regulatory mechanisms.
The AGPAT2 genes is expressed mainly within the liver and adipose. There are three isoforms of AGPAT: AGPAT1 is highly expressed in the liver and adipocytes, AGPAT2 is poorly expressed in the liver and adipocyte tissue, and AGPAT3 is absent. The molecular roles of the AGPAT2 mark are currently unknown.
AGPAT2 and CDS1/2 have a functional relationship that is unique to them. This relationship is partly responsible to abnormal LD formation of cells lacking AGPAT2.
This gene plays an essential role in adipogenesis. Mutations in AGPAT2 expression can lead to insulin resistance and generalised lipodystrophy. The current study looked at the role of AGPAT2 variants in adipogenic deformities in mice. Muscle-derived multipotent muscle cells were isolated using vastus lateralis biopsies. They were then cultured as 3T3–L1 preadipocytes.
Knockdown AGPAT2 led to a decrease of oleate in PG. PI. and TAG. Overexpressions of AGPAT2 reduced oleate integration into PG and Pi, while knocking down AGPAT1 had very little effect on lipid flow. The global Agpat2-deficient mice's LD sizes were similar to those of the controls. The mice had normal GIs, and their liver weights.
AGPAT2 can interact with CDS1/2 and CDS2-CDS1/2. AGPAT2-GFP and CDS1-CDS2 co-immunoprecipitate with equal affinity in human CDS1/2. Seipin, another AGPAT Protein, interacts with GPAT4 and not AGPAT2.
AGPAT2 can be found in the endoplasmicreticulum. It catalyzes the conversion of lysophosphatidic a to phosphatidic, which is a precursor for triacylglycerols and triglycerides. AGPAT2 deficiency leads to decreased adipocyte growth and defective signaling of key elements such as PI3K/AKT or PPARg which can lead to abnormal adipogenesis.
The AGPAT2 gene codes for a protein that is found in many tissues throughout the body. This enzyme is crucial for the development and maintenance of adipocytes. Adipocytes store fat for energy, and contribute to the overall body fat. This enzyme is part of a chemical pathway in many different types of cells, generating two different types of lipids: glycerophospholipids and triacylglycerols. Glycerophospholipids are essential components of cell membranes, while triacylglycerides (fat molecules that regulate chemical signals in cells) are key components of cell membranes.
AGPAT2 a protein that is associated with CDS1/2 in a specific way. AGPAT2 was demonstrated to interact with CDS1 (and CDS2) in HEK293F cell lines. It interacts with CDS1/2, HA-CDS and CDS1/2 in HEK293E cell. Furthermore, aGPAT2-GFP protein was found interact with Strep-tagged CDS1 in HEK293F cells.
AGPAT2 knockdown cells in HeLa cells were able rescue the LD phenotype when expressed in the absence H98A. AGPAT2 knockdown in 3T3 L1 cells increased the size of LDs but did not decrease cell viability. CDS1 and seipin were overexpressed in 3T3 L1 adipocytes. This reduced cellular PA and prevented the formation of LDs larger than normal in AGPAT2-deficient cells.
AGPAT2 is located in the ER10 in human cells. However, it has not been identified due to the absence of an anti-AGPAT2 antibodies. The fluorescence signal of AGPAT2-sfGFP colocalized well with the calnexin marker, which is a marker of ER. The fluorescence signal vanished after knockdown by siRNA of AGPAT2, confirming the accuracy and integration of GFP.
AGPAT2 can interact directly with CDS1/2 and form functional complexes which promote PA metabolism in CDP-DAG. These interactions provide crucial insight into metabolic flux regulation. The findings suggest that AGPAT2 is involved in substrate channelling at the branch point of the glycerol-3 phosphate pathway. It is also suggested that AGPAT2 may be involved in the metabolism and synthesis of phospholipids.
Adipocyte differentiation does not require AGPAT2 to be expressed, but AGPAT2 overexpression causes Lipin-1 to be expelled from the nuclear genome. This result is consistent with the presence of an increase in PA in the endoplasmic reticulum. These complex changes require further study. However, changes in AGPAT2 could cause unexpected changes to lipid metabolism.
Low insulin levels are not affected by AGPAT2. Akt is phosphorylated by AGPAT2. This is critical for the production or adipocyte-derived adipogenic hormones. AGPAT2 is required for cell death. However, increased Akt phosphorylation leads to an increase in adiponectin level in the adipocytes. It is crucial to examine AGPAT2 in order to identify fat cells that are cancerous.
AGPAT2 regulates adipogenesis for both CGL and normal patients. Berardinelli-Seip has been linked to this gene. Moreover, mutations in AGPAT2 are associated with adipogenesis and hypertriglyceridemia. Further studies are needed in order to determine whether AGPAT2 is responsible for lipodystrophy.
The AGPAT2 genes provides instructions for an enzyme found in many tissues throughout our bodies. It is essential for the development of adipocytes. These cells store fat for energy. AGPAT2 enzyme is part a chemical pathway that produces two types lipids: triacylglycerols and glycerophospholipids. Glycerophospholipids make up the majority of cell membranes, and triacylglycerols make up fat molecules that play an important part in chemical signaling within cells.
PMID: 9242711 by Eberhardt C., et al. Human lysophosphatidic acid acyltransferase. cDNA cloning, expression, and localization to chromosome 9q34.3.
PMID: 9291118 by Stamps A.C., et al. A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases.