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Literature summary for 3.1.3.4 extracted from
- Lipin - The bridge between hepatic glycerolipid biosynthesis and lipoprotein metabolism (2010), Biochim. Biophys. Acta, 1801, 1249-1259.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytoplasm | isoform lipin-1beta | Mus musculus | 5737 | - |
| cytoplasm | isoform lipin-1beta | Homo sapiens | 5737 | - |
| cytoplasm | isoform lipin-1beta | Rattus norvegicus | 5737 | - |
| membrane | microsome | Mus musculus | 16020 | - |
| membrane | microsome | Homo sapiens | 16020 | - |
| membrane | microsome | Rattus norvegicus | 16020 | - |
| nucleus | isoform lipin-1alpha | Mus musculus | 5634 | - |
| nucleus | isoform lipin-1alpha | Homo sapiens | 5634 | - |
| nucleus | isoform lipin-1alpha | Rattus norvegicus | 5634 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | dependent on | Mus musculus |  |
| Mg2+ | dependent on | Homo sapiens | |
| Mg2+ | dependent on | Rattus norvegicus | |
| Mn2+ | dependent on | Mus musculus | |
| Mn2+ | dependent on | Homo sapiens | |
| Mn2+ | dependent on | Rattus norvegicus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
| Mus musculus | - |
- |
- |
| Rattus norvegicus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | insulin-stimulated phosphorylation sites in lipin-1 are at Ser106, Ser634, and Ser720 | Mus musculus |
| phosphoprotein | insulin-stimulated phosphorylation sites in lipin-1 are at Ser106, Ser634, and Ser720 | Homo sapiens |
| sumoylation | isoforms lipin-1alpha and lipin-1beta undergo sumoylation on two consensus sumoylation sites | Mus musculus |
| sumoylation | isoforms lipin-1alpha and lipin-1beta undergo sumoylation on two consensus sumoylation sites | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| 3T3-L1 cell | - |
Mus musculus | - |
| adipocyte | - |
Mus musculus | - |
| adipocyte | - |
Homo sapiens | - |
| brown adipose tissue | - |
Mus musculus | - |
| brown adipose tissue | - |
Homo sapiens | - |
| brown adipose tissue | - |
Rattus norvegicus | - |
| cerebral cortical neuron | - |
Mus musculus | - |
| cerebral cortical neuron | - |
Homo sapiens | - |
| embryo | - |
Mus musculus | - |
| embryo | - |
Homo sapiens | - |
| HEK-293 cell | - |
Homo sapiens | - |
| HeLa cell | - |
Homo sapiens | - |
| liver | - |
Mus musculus | - |
| liver | - |
Homo sapiens | - |
| liver | - |
Rattus norvegicus | - |
| McA-RH7777 cell | - |
Rattus norvegicus | - |
| SH-SY5Y cell | - |
Homo sapiens | - |
| skeletal muscle | - |
Mus musculus | - |
| skeletal muscle | - |
Homo sapiens | - |
| skeletal muscle | - |
Rattus norvegicus | - |
| white adipose tissue | - |
Mus musculus | - |
| white adipose tissue | - |
Homo sapiens | - |
| white adipose tissue | - |
Rattus norvegicus | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| lipin 1 | - |
Mus musculus |
| lipin 1 | - |
Homo sapiens |
| lipin 1 | - |
Rattus norvegicus |
| lipin-1alpha | isoform | Mus musculus |
| lipin-1alpha | isoform | Homo sapiens |
| lipin-1alpha | isoform | Rattus norvegicus |
| lipin-1beta | isoform | Mus musculus |
| lipin-1beta | isoform | Homo sapiens |
| lipin-1beta | isoform | Rattus norvegicus |
| lipin-1gamma | isoform | Mus musculus |
| lipin-1gamma | isoform | Homo sapiens |
| lipin-1gamma | isoform | Rattus norvegicus |
| LPIN1 | - |
Mus musculus |
| LPIN1 | - |
Homo sapiens |
| LPIN1 | - |
Rattus norvegicus |
| PAP | - |
Mus musculus |
| PAP | - |
Homo sapiens |
| PAP | - |
Rattus norvegicus |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Mus musculus | hepatic lipin-1 expression is selectively repressed by insulin | down |
| Homo sapiens | hepatic lipin-1 expression is selectively repressed by insulin | down |
| Homo sapiens | hepatic lipin-1 expression is selectively stimulated by glucocorticoids. The expression of lipin-1 is markedly up-regulated under stress conditions | up |
| Mus musculus | hepatic lipin-1 expression is selectively stimulated by glucocorticoids. The expression of lipin-1 is markedly upregulated under stress conditions | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | fatty liver dystrophy mice carrying mutations within the lipin 1 gene display life-long deficiency in adipogenesis, insulin resistance, neonatal hepatosteatosis and hypertriglyceridemia, as well as increased atherosclerosis susceptibility. Lipin-1 deficiency results in the activation of the sterol regulatory element binding protein 1 and its target genes as well as in very high expression levels of stearoyl-CoA desaturase-1 and apoA-IV. Acute lipin-1 deficiency in the mouse liver abolishes fasting-induced activation of Ppara and several PPARalpha/PGC-1alpha target genes, such as Acadvl, Acadm and Fabp1 | Mus musculus |
| malfunction | lipin-1 deficiency in humans is not associated with lipodystrophy. In HeLa cells, knockdown of lipin-2 results in increased phosphatidate phosphatase activity, apparently as a result of compensatory upregulation of lipin-1 | Homo sapiens |
| physiological function | lipin proteins play a dual function in lipid metabolism by acting as phosphatidate phosphatase enzymes and as transcriptional regulators. Lipin-1 is a key integrator of hormonal signals to the liver in diabetic dyslipidemia. Lipin-1 also induces the expression of key adipogenic transcription factors including PPARgamma and C/EBPalpha. Isoforms lipin-1alpha and lipin-1beta exert complementary roles in adipocyte differentiation. While lipin-1alpha induces the expression of adipogenic transcription factors, lipin-1beta induces the expression of lipid synthesis genes encoding, e.g., fatty acid synthase and diacylglycerol acyltransferase. Hepatic very low density lipoprotein synthesis and secretion is highly influenced by the expression of lipin-1. Membrane dynamics (conveyor) for very low density lipoprotein assembly/secretion are regulated by lipin-1 | Mus musculus |
| physiological function | lipin proteins play a dual function in lipid metabolism by acting as phosphatidate phosphatase enzymes and as transcriptional regulators. Lipin-1 is a key integrator of hormonal signals to the liver in diabetic dyslipidemia. Lipin-1 also induces the expression of key adipogenic transcription factors including PPARgamma and C/EBPalpha. Isoforms lipin-1alpha and lipin-1beta exert complementary roles in adipocyte differentiation. While lipin-1alpha induces the expression of adipogenic transcription factors, lipin-1beta induces the expression of lipid synthesis genes encoding, e.g., fatty acid synthase and diacylglycerol acyltransferase. Hepatic very low density lipoprotein synthesis and secretion is highly influenced by the expression of lipin-1. Membrane dynamics (conveyor) for very low density lipoprotein assembly/secretion are regulated by lipin-1 | Homo sapiens |
| physiological function | lipin proteins play a dual function in lipid metabolism by acting as phosphatidate phosphatase enzymes and as transcriptional regulators. Lipin-1 is a key integrator of hormonal signals to the liver in diabetic dyslipidemia. Lipin-1 also induces the expression of key adipogenic transcription factors including PPARgamma and C/EBPalpha. Isoforms lipin-1alpha and lipin-1beta exert complementary roles in adipocyte differentiation. While lipin-1alpha induces the expression of adipogenic transcription factors, lipin-1beta induces the expression of lipid synthesis genes encoding, e.g., fatty acid synthase and diacylglycerol acyltransferase. Hepatic very low density lipoprotein synthesis and secretion is highly influenced by the expression of lipin-1. Membrane dynamics (conveyor) for very low density lipoprotein assembly/secretion are regulated by lipin-1 | Rattus norvegicus |
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