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Literature summary for 2.3.1.15 extracted from

  • Lee, J.; Ridgway, N.
    Substrate channeling in the glycerol-3-phosphate pathway regulates the synthesis, storage and secretion of glycerolipids (2020), Biochim. Biophys. Acta, 1865, 158438 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information changes in GPAT4 activity in overexpressing Cos-7 cells and knockout mice Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
N-ethylmaleimide
-
Homo sapiens
N-ethylmaleimide
-
Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum membrane
-
Mus musculus 5789
-
endoplasmic reticulum membrane
-
Homo sapiens 5789
-
microsome
-
Mus musculus
-
-
microsome
-
Homo sapiens
-
-
mitochondrial outer membrane
-
Mus musculus 5741
-
mitochondrial outer membrane
-
Homo sapiens 5741
-
additional information in most tissues, GPAT3 and/or GPAT4 activity in the endoplasmic reticulum is 10fold greater than mitochondrial activity Mus musculus
-
-
additional information in most tissues, GPAT3 and/or GPAT4 activity in the endoplasmic reticulum is 10fold greater than mitochondrial activity Homo sapiens
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acyl-CoA + sn-glycerol 3-phosphate Mus musculus
-
CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + sn-glycerol 3-phosphate Homo sapiens
-
CoA + 1-acyl-sn-glycerol 3-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q53EU6
-
-
Homo sapiens Q6NUI2
-
-
Homo sapiens Q86UL3
-
-
Homo sapiens Q9HCL2
-
-
Mus musculus Q14DK4
-
-
Mus musculus Q61586
-
-
Mus musculus Q8C0N2
-
-
Mus musculus Q8K2C8
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein in 3T3-L1 adipocytes, GPAT3 and GPAT4 activity is stimulated by insulin-dependent phosphorylation of serine and threonine residues Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
3T3-L1 cell
-
Mus musculus
-
adipocyte
-
Mus musculus
-
adipocyte
-
Homo sapiens
-
brain
-
Mus musculus
-
brain
-
Homo sapiens
-
brown adipose tissue
-
Mus musculus
-
brown adipose tissue
-
Homo sapiens
-
colon
-
Mus musculus
-
colon
-
Homo sapiens
-
heart
-
Mus musculus
-
heart
-
Homo sapiens
-
intestine
-
Mus musculus
-
intestine
-
Homo sapiens
-
kidney
-
Mus musculus
-
kidney
-
Homo sapiens
-
liver
-
Mus musculus
-
liver
-
Homo sapiens
-
lung
-
Mus musculus
-
lung
-
Homo sapiens
-
lung lowest expression level Mus musculus
-
additional information expression pattern of GPAT isozymes, overview Mus musculus
-
additional information expression pattern of GPAT isozymes, overview Homo sapiens
-
muscle
-
Mus musculus
-
muscle
-
Homo sapiens
-
skeletal muscle
-
Mus musculus
-
skeletal muscle
-
Homo sapiens
-
small intestine
-
Mus musculus
-
small intestine
-
Homo sapiens
-
testis
-
Mus musculus
-
testis
-
Homo sapiens
-
white adipose tissue
-
Mus musculus
-
white adipose tissue
-
Homo sapiens
-
white adipose tissue highest expression level Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + sn-glycerol 3-phosphate
-
Mus musculus CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + sn-glycerol 3-phosphate
-
Homo sapiens CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + sn-glycerol 3-phosphate acyl-CoA specificity of GPAT1 is 16:0 > 18:0 > 18:1 Mus musculus CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + sn-glycerol 3-phosphate acyl-CoA specificity of GPAT1 is 16:0 > 18:0 > 18:1 Homo sapiens CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + sn-glycerol 3-phosphate GPAT2 shows no acyl-CoA specificity Mus musculus CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + sn-glycerol 3-phosphate GPAT2 shows no acyl-CoA specificity Homo sapiens CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + sn-glycerol 3-phosphate GPAT3 shows a specificity for 16:0, 18:1, 18:2 acyl-CoAs Mus musculus CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + sn-glycerol 3-phosphate GPAT3 shows a specificity for 16:0, 18:1, 18:2 acyl-CoAs Homo sapiens CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + sn-glycerol 3-phosphate GPAT4 shows no acyl-CoA specificity Mus musculus CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
acyl-CoA + sn-glycerol 3-phosphate GPAT4 shows no acyl-CoA specificity Homo sapiens CoA + 1-acyl-sn-glycerol 3-phosphate
-
?

Synonyms

Synonyms Comment Organism
AGPAT6 fomerly Mus musculus
AGPAT6 fomerly Homo sapiens
glycerol-3-phosphate acyltransferase
-
Mus musculus
glycerol-3-phosphate acyltransferase
-
Homo sapiens
GPAT1
-
Mus musculus
GPAT1
-
Homo sapiens
GPAT2
-
Mus musculus
GPAT2
-
Homo sapiens
GPAT3
-
Mus musculus
GPAT3
-
Homo sapiens
GPAT4
-
Mus musculus
GPAT4
-
Homo sapiens

Expression

Organism Comment Expression
Mus musculus isozyme Gpat3 mRNA is increased about 60fold during 3T3-L1 differentiation as a result of transcriptional activation by peroxisome proliferator-activated receptor gamma (PPARgamma) up

General Information

General Information Comment Organism
malfunction Gpat3-/- mice have about 80% reduction in GPAT activity in white adipose tissue, are resistant to weight gain and have improved insulin sensitivity in response to a high-fat diet. In enterocytes from Gpat3-/- mice, excess fatty acids are oxidized and esterified to cholesterol, which are stored and secreted in chylomicrons. Gpat3-/- mice fed a high-fat diet have decreased weight gain, fat mass and enlarged livers, indicating an important role in fatty acid storage in white adipose tissue. Liver enlargement in Gpat3-/- mice is due to cholesterol ester storage resulting from dysregulation of intestinal cholesterol secretion. Overexpression of endoplasmic reticulum-localized GPAT3 or GPAT4 in cultured cells does not affect incorporation of exogenous fatty acids into the major phospholipid classes Mus musculus
malfunction overexpression of endoplasmic reticulum-localized GPAT3 or GPAT4 in cultured cells does not affect incorporation of exogenous fatty acids into the major phospholipid classes Homo sapiens
malfunction overexpression of GPAT1 in CHO, HEK-293 and primary rodent hepatocytes is sufficient to increase fatty acid incorporation into triglycerides and phospholipids. Gpat1-/- mice have a severe block in hepatic de novo synthesis of total phospholipids. Knockout of GPAT1 activity in cardiomyocytes and hepatocytes increases the arachidonate and oleate content of phosphocholine and phosphoethanolamine. Gpat1-/- mice are less susceptible to carcinogen-induced liver tumorigenesis. Gpat1-/- mice fed a high-sucrose diet to stimulate de novo lipogenesis have a 50% reduction in hepatic and plasma triglycerides, increased hepatic content of long-chain acylcarnitines and reduced very low density lipoprotein (VLDL) secretions. Liver-specific adenoviral expression of GPAT1 results in triglycerides and diacylglycerol accumulation, decreased fatty acid beta-oxidation, and hyperlipidemia Mus musculus
malfunction overexpression of GPAT1 in CHO, HEK-293 and primary rodent hepatocytes is sufficient to increase fatty acid incorporation into triglycerides and phospholipids. Knockout of GPAT1 activity in cardiomyocytes and hepatocytes increases the arachidonate and oleate content of phosphocholine and phosphoethanolamine Homo sapiens
malfunction the liver and brown adipose tissue of Gpat4-/- mice have a 65% reduction in NEM-sensitive GPAT activity, but activity in white adipose tissue is unaffected due to high levels of GPAT3 expression. Female Gpat4-/- mice fed a high-fat diet have increased PPARgamma-mediated Ucp1 expression and thermogenesis in brown adipose tissue resulting from elevated acyl-CoAs due to diminished esterification. Incorporation of exogenous oleate into phospholipid is unaffected in tissues of Gpat4-/- mice. Overexpression of endoplasmic reticulum-localized GPAT3 or GPAT4 in cultured cells does not affect incorporation of exogenous fatty acids into the major phospholipid classes Mus musculus
metabolism substrate channeling in the glycerol-3-phosphate pathway regulates the synthesis, storage and secretion of glycerolipids. The successive acylation of glycerol-3-phosphate (G3P) by glycerol-3-phosphate acyltransferases and acylglycerol-3-phosphate acyltransferases produces phosphatidic acid (PA), a precursor for CDP-diacylglycerol-dependent phospholipid synthesis. PA is further dephosphorylated by LIPINs to produce diacylglycerol (DG), a substrate for the synthesis of triglyceride (TG) by DG acyltransferases and a precursor for phospholipid synthesis via the CDP-choline and CDP-ethanolamine (Kennedy) pathways. The channeling of fatty acids into TG for storage in lipid droplets and secretion in lipoproteins or phospholipids for membrane biogenesis is dependent on isoform expression, activity and localization of G3P pathway enzymes, as well as dietary and hormonal and tissue-specific factors. Mechanisms that control partitioning of substrates into lipid products of the G3P pathway, overview Mus musculus
metabolism substrate channeling in the glycerol-3-phosphate pathway regulates the synthesis, storage and secretion of glycerolipids. The successive acylation of glycerol-3-phosphate (G3P) by glycerol-3-phosphate acyltransferases and acylglycerol-3-phosphate acyltransferases produces phosphatidic acid (PA), a precursor for CDP-diacylglycerol-dependent phospholipid synthesis. PA is further dephosphorylated by LIPINs to produce diacylglycerol (DG), a substrate for the synthesis of triglyceride (TG) by DG acyltransferases and a precursor for phospholipid synthesis via the CDP-choline and CDP-ethanolamine (Kennedy) pathways. The channeling of fatty acids into TG for storage in lipid droplets and secretion in lipoproteins or phospholipids for membrane biogenesis is dependent on isoform expression, activity and localization of G3P pathway enzymes, as well as dietary and hormonal and tissue-specific factors. Mechanisms that control partitioning of substrates into lipid products of the G3P pathway, overview Homo sapiens
physiological function GPAT1 dictates fatty acid composition at the level of AGPATs or by acyl-chain remodeling by lysophospholipid acyltransferases (LPLATs). GPAT1 determines the metabolic fate of exogenous fatty acids Mus musculus
physiological function GPAT1 dictates fatty acid composition at the level of AGPATs or by acyl-chain remodeling by lysophospholipid acyltransferases (LPLATs). GPAT1 determines the metabolic fate of exogenous fatty acids Homo sapiens
physiological function isozyme GPAT3 is primarily involved in triglyceride (TG) storage in adipocytes. Contribution of GPATs to acyl-CoA partitioning into glycerolipid synthesis and beta-oxidation Mus musculus
physiological function isozyme GPAT3 is primarily involved in triglyceride (TG) storage in adipocytes. Contribution of GPATs to acyl-CoA partitioning into glycerolipid synthesis and beta-oxidation, overview Homo sapiens
physiological function isozyme GPAT4 is a primary contributor to lysophosphatidic acid synthesis in liver and brown adipose tissue. Contribution of GPATs to acyl-CoA partitioning into glycerolipid synthesis and beta-oxidation Homo sapiens
physiological function isozyme GPAT4 is a primary contributor to lysophosphatidic acid synthesis in liver and brown adipose tissue. Contribution of GPATs to acyl-CoA partitioning into glycerolipid synthesis and beta-oxidation. GPAT4 expression and high-fat diet-induced insulin resistance are linked to altered levels of palmitate-enriched phosphatidic acid and diacylglycerol and altered mTORC2 Mus musculus