LPIN1 encodes lipin-1, a Mg2+-dependent phosphatidate phosphatase (PAP1; EC 3.1.3.4) that catalyzes the penultimate step of glycerolipid synthesis, the dephosphorylation of phosphatidic acid (PA) to diacylglycerol (DAG) plus inorganic phosphate. DAG produced by lipin-1 is the shared precursor for triacylglycerol and for the glycerophospholipids phosphatidylcholine and phosphatidylethanolamine, so lipin-1 sits at a branch point controlling both neutral-lipid storage and membrane-phospholipid production. Lipin-1 belongs to the lipin family, has a haloacid dehalogenase (HAD)-like catalytic domain bearing the DxDxT motif, and is not an integral membrane protein; it is largely cytosolic and translocates onto the endoplasmic reticulum (and nuclear) membrane surface to act on its lipid substrate, with membrane association governed by its phosphorylation state (mTOR-dependent phosphorylation being inhibitory) and by KAT5/Tip60-mediated acetylation. Lipin-1 is bifunctional: beyond its enzymatic role it acts in the nucleus as a transcriptional coactivator/corepressor of lipid-metabolism genes, notably in the PGC-1alpha/PPARalpha regulatory pathway. It is most abundant in skeletal muscle and adipose tissue. Biallelic loss-of-function LPIN1 mutations cause recurrent acute myoglobinuria (severe childhood rhabdomyolysis), and in mouse the orthologous gene (fld) underlies lipodystrophy.
Definition: Existing term GO:0006651 (diacylglycerol biosynthetic process) should be added as an involved_in annotation for LPIN1; lipin-1 directly generates diacylglycerol by dephosphorylating phosphatidic acid.
Justification: Lipin-1's immediate catalytic product is diacylglycerol; capturing the DAG biosynthetic process (in addition to the downstream triglyceride biosynthetic process) would more precisely represent the enzyme's direct metabolic output.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005634 nucleus | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Lipin-1 has a documented nuclear pool where it acts as a transcriptional coregulator; the founding fld/lipin paper described it as a nuclear protein. This nuclear localization is real but non-core relative to the PAP enzymatic function on cytosolic/ER membranes. Supporting Evidence: PMID:11138012 The gene (Lpin1) encodes a novel nuclear protein which we have named lipin. |
| GO:0008195 phosphatidate phosphatase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Core, correct molecular function. Phylogenetic (IBA) inference of the PAP1 activity that is directly demonstrated for the human protein by multiple experimental studies. Retained as the central function. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol |
| GO:0009062 fatty acid catabolic process | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: Phylogenetically inferred involvement in fatty acid catabolism. Lipin-1's direct catalytic role is in glycerolipid biosynthesis (PA to DAG), not fatty acid breakdown; any link to catabolism is indirect (via the transcriptional coactivation of fatty-acid-oxidation genes in the PGC-1alpha/PPARalpha pathway). Better captured by the transcriptional-coactivator annotations; this direct-catabolism term is peripheral. |
| GO:0019432 triglyceride biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: Core biological process. Lipin-1 produces the DAG that is the immediate precursor of triacylglycerol; this is directly demonstrated experimentally for the human protein (PMID:29765047) and phylogenetically conserved. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis |
| GO:0005741 mitochondrial outer membrane | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Lipin-1 can be recruited to the mitochondrial outer membrane and participate in mitochondrial dynamics/proteostasis by locally converting PA to DAG (mTORC1-LIPIN1-YME1L axis lowers mitochondrial PE). This is a genuine but secondary, non-core localization/role. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt Recruited at the mitochondrion outer membrane and is involved in mitochondrial fission by converting phosphatidic acid to diacylglycerol |
| GO:0003713 transcription coactivator activity | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Genuine second (moonlighting) function: nuclear lipin-1 acts as a transcriptional coactivator/coregulator in the PGC-1alpha/PPARalpha pathway (LXXIL motif interaction with PPARA). Well supported at the family/ortholog level (By similarity) but direct human evidence is limited, so kept as a non-core function distinct from the primary PAP enzymatic role. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt Acts also as nuclear transcriptional coactivator for PPARGC1A/PPARA regulatory pathway to modulate lipid metabolism gene expression |
| GO:0032869 cellular response to insulin stimulus | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Lipin-1 activity and localization are regulated by insulin/mTOR signaling (mTOR phosphorylates lipin-1, inactivating it). Being downstream of insulin signaling is a real regulatory context but not a core function of the gene product itself. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt Phosphorylated at multiple sites by mTOR in response to insulin, leading to its inactivation |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Consequence of lipin-1's nuclear transcriptional-coactivator activity on lipid-metabolism target genes. Real but non-core (moonlighting nuclear function), consistent with the transcription coactivator activity annotation. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt Acts also as nuclear transcriptional coactivator for PPARGC1A/PPARA regulatory pathway to modulate lipid metabolism gene expression |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Correct core localization. Lipin-1 translocates from cytosol onto the ER membrane to access its lipid substrate; experimentally supported for the human protein (PMID:29765047) and captured by UniProt subcellular location. IEA mapping is redundant with, and consistent with, the experimental annotation. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt Endoplasmic reticulum membrane {ECO:0000269|PubMed:29765047}. |
| GO:0005829 cytosol | IEA GO_REF:0000044 | ACCEPT | Summary: Correct core localization. Lipin-1 is a soluble (non-integral-membrane) protein predominantly cytosolic in the resting state, translocating to membranes to act; experimentally supported for the human protein. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt Cytoplasm, cytosol {ECO:0000269|PubMed:29765047}. |
| GO:0008195 phosphatidate phosphatase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Core molecular function, here inferred electronically from RHEA/EC mappings. Directly demonstrated experimentally for the human protein; ACCEPT rather than flag as redundant IEA because this is the gene's own central function. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol |
| GO:0031965 nuclear membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Nuclear membrane localization is annotated By similarity (from mouse) and reflects the regulated nuclear/nuclear-envelope pool where lipin-1 is dephosphorylated by the CTDNEP1-CNEP1R1 complex. Real but non-core relative to the cytosol/ER catalytic pool. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt Nucleus membrane {ECO:0000250|UniProtKB:Q91ZP3}. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | MARK AS OVER ANNOTATED | Summary: Bare "protein binding" from a large-scale yeast two-hybrid neurodegenerative disease interactome screen (LPIN1 was one of ~500 ND-related baits; reported partners include HTT, ATXN10, WFS1). Uninformative about lipin-1's function and not indicative of a specific physiological complex; over-annotation. Not removed per policy for experimental IPI protein-binding annotations. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects ~5,000 human proteins via ~30,000 candidate interactions |
| GO:0031100 animal organ regeneration | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Electronic transfer from a single rat ortholog (Ensembl Compara). Not supported by any human/lipin-1-specific evidence and unrelated to lipin-1's characterized catalytic or transcriptional functions; a peripheral single-ortholog over-annotation. |
| GO:0031642 negative regulation of myelination | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Electronic transfer from a single rat ortholog. Lipin-1 does have roles in peripheral nerve/Schwann cell lipid metabolism (fld mice have peripheral neuropathy), but this specific "negative regulation of myelination" term is an ortholog-transferred inference without direct human support; peripheral over-annotation. |
| GO:0032869 cellular response to insulin stimulus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Duplicate of the IBA cellular-response-to-insulin annotation, here by Ensembl ortholog transfer. Real regulatory context (mTOR/insulin controls lipin-1 phosphorylation) but non-core. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt Phosphorylated at multiple sites by mTOR in response to insulin, leading to its inactivation |
| GO:1905694 negative regulation of phosphatidic acid biosynthetic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: By consuming phosphatidic acid (converting it to DAG), lipin-1 lowers cellular PA levels, so this regulatory term is mechanistically plausible and consistent with the PAP reaction. It is an ortholog-transferred (IEA) restatement of the direct catalytic role; kept as non-core rather than a core function statement, which is better captured by the PAP activity and phosphatidic acid metabolic process. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt catalyzes the conversion of phosphatidic acid to diacylglycerol |
| GO:0007077 mitotic nuclear membrane disassembly | TAS Reactome:R-HSA-2980766 | KEEP AS NON CORE | Summary: Reactome-derived pathway annotation for the nuclear-envelope context in which lipin-1/PAP is dephosphorylated (by CDK1) during mitosis. Lipin-1 PAP1 activity is indeed inhibited by mitotic phosphorylation, but a direct role in executing nuclear membrane disassembly is a pathway-level assertion, not a core lipin-1 function; keep as non-core. Supporting Evidence: PMID:18694939 the PAP1 activity of both lipins is inhibited by phosphorylation during mitosis |
| GO:0019432 triglyceride biosynthetic process | TAS Reactome:R-HSA-75109 | ACCEPT | Summary: Core biological process (Reactome "Triglyceride biosynthesis"). Lipin-1 generates DAG, the penultimate intermediate of TAG synthesis. Consistent with the experimental IDA annotation. Supporting Evidence: PMID:29765047 the dephosphorylation of phosphatidic acids (PAs) to form diacylglycerols (DAGs), the penultimate step in TAG synthesis |
| GO:0008195 phosphatidate phosphatase activity | EXP PMID:18694939 Temporal and spatial regulation of the phosphatidate phospha... | ACCEPT | Summary: Experimental support for lipin-1 PAP1 activity: siRNA depletion of lipin 1 removes ~86% of cellular Mg2+-dependent PAP1 activity in HeLa cells, identifying it as the major PAP1 enzyme. Core function; ACCEPT. Supporting Evidence: PMID:18694939 lipin 1-depleted extracts show an 86% reduction in the total cellular PAP1 activity, indicating that lipin 1 is the major PAP1 enzyme in these cells |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:29765047 Tip60-mediated lipin 1 acetylation and ER translocation dete... | ACCEPT | Summary: Experimentally demonstrated ER-membrane localization: fatty-acid-induced, KAT5/Tip60-dependent acetylation drives cytosol-to-ER translocation of lipin-1 to generate DAG for TAG synthesis. Core localization for catalysis. Supporting Evidence: PMID:29765047 it needs to translocate from cytosol to endoplasmic reticulum (ER) membranes, whereby the hydrophobic phospholipids and neutral lipids are synthesized |
| GO:0008195 phosphatidate phosphatase activity | EXP PMID:20231281 Characterization of the human LPIN1-encoded phosphatidate ph... | ACCEPT | Summary: Direct biochemical characterization of purified human lipin-1 alpha/beta/gamma isoforms as Mg2+/Mn2+-dependent PA phosphatases with defined kinetics. Strong core-function evidence; ACCEPT. Supporting Evidence: PMID:20231281 PA phosphatase activities of the alpha, beta, and gamma isoforms were dependent on Mg(2+) or Mn(2+) ions at pH 7.5 at 37 degrees C. |
| GO:0008195 phosphatidate phosphatase activity | EXP PMID:39577771 The antidepressant drug sertraline is a novel inhibitor of y... | ACCEPT | Summary: Human lipin-1 (alpha/beta/gamma) PAP activity confirmed and characterized as an inhibitor target (sertraline, propranolol). Reinforces the core PAP molecular function; ACCEPT. Supporting Evidence: PMID:39577771 Sertraline also inhibited the PAP activity of human lipin 1 |
| GO:0031965 nuclear membrane | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Nuclear-membrane localization inferred from the mouse ortholog (Q91ZP3). Reflects the regulated nuclear/nuclear-envelope pool; real but non-core relative to the cytosol/ER catalytic pool. Duplicate of the IEA nuclear membrane annotation. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt Nucleus membrane {ECO:0000250|UniProtKB:Q91ZP3}. |
| GO:0008195 phosphatidate phosphatase activity | IDA PMID:23426360 Phosphorylation of lipin 1 and charge on the phosphatidic ac... | ACCEPT | Summary: Direct assay of lipin-1 PAP activity (PA/PE micelle assay) and its regulation by phosphorylation and PA head-group charge. Core molecular function; ACCEPT. Supporting Evidence: PMID:23426360 The lipin gene family encodes a class of Mg(2+)-dependent phosphatidic acid phosphatases involved in the de novo synthesis of phospholipids and triglycerides. |
| GO:0008195 phosphatidate phosphatase activity | IDA PMID:31695197 Lipid signalling drives proteolytic rewiring of mitochondria... | ACCEPT | Summary: LIPIN1 PAP activity acting on mitochondrial membrane lipids (lowering PE) in the mTORC1-LIPIN1-YME1L axis. Direct evidence for the core PAP function; ACCEPT. Supporting Evidence: PMID:31695197 a lipid signalling cascade via the phosphatidic acid phosphatase LIPIN1, which decreases phosphatidylethanolamine levels in mitochondrial membranes |
| GO:0046337 phosphatidylethanolamine metabolic process | IDA PMID:23426360 Phosphorylation of lipin 1 and charge on the phosphatidic ac... | ACCEPT | Summary: Lipin-1 acts in phosphatidylethanolamine metabolism because the DAG it produces is the precursor for PE (and PC) synthesis, and the in-vitro assay here specifically uses PA/PE mixtures. Genuine downstream metabolic role; ACCEPT as a (non-primary) biological process. Supporting Evidence: PMID:23426360 Mg(2+)-dependent phosphatidic acid phosphatases involved in the de novo synthesis of phospholipids and triglycerides |
| GO:0046337 phosphatidylethanolamine metabolic process | IDA PMID:31695197 Lipid signalling drives proteolytic rewiring of mitochondria... | ACCEPT | Summary: Directly supported: LIPIN1 activity decreases phosphatidylethanolamine levels in mitochondrial membranes, placing it in PE metabolism. ACCEPT. Supporting Evidence: PMID:31695197 which decreases phosphatidylethanolamine levels in mitochondrial membranes and promotes proteolysis |
| GO:0005783 endoplasmic reticulum | IDA PMID:29765047 Tip60-mediated lipin 1 acetylation and ER translocation dete... | ACCEPT | Summary: Experimentally supported active site of catalysis: lipin-1 translocates to the ER to generate DAG for lipid synthesis. Core localization; ACCEPT. Supporting Evidence: PMID:29765047 it needs to translocate from cytosol to endoplasmic reticulum (ER) membranes, whereby the hydrophobic phospholipids and neutral lipids are synthesized |
| GO:0005829 cytosol | IDA PMID:29765047 Tip60-mediated lipin 1 acetylation and ER translocation dete... | ACCEPT | Summary: Experimentally supported cytosolic localization (the resting/soluble pool before membrane translocation). Consistent with lipin-1 being a non-integral-membrane protein. Core; ACCEPT. Supporting Evidence: PMID:18694939 lipin 1-HA shows a predominantly cytosolic staining |
| GO:0008195 phosphatidate phosphatase activity | IDA PMID:29765047 Tip60-mediated lipin 1 acetylation and ER translocation dete... | ACCEPT | Summary: Direct evidence for lipin-1 PAP activity (generating DAG at the ER for TAG synthesis). Core molecular function; ACCEPT. Supporting Evidence: PMID:29765047 endoplasmic reticulum translocation of |
| GO:0019432 triglyceride biosynthetic process | IDA PMID:29765047 Tip60-mediated lipin 1 acetylation and ER translocation dete... | ACCEPT | Summary: Direct experimental evidence that lipin-1 acetylation/ER translocation determines the rate of triacylglycerol synthesis. Core biological process; ACCEPT. Supporting Evidence: PMID:29765047 to generate diacylglycerol for TAG |
| GO:0120162 positive regulation of cold-induced thermogenesis | ISS PMID:23028044 Cell autonomous lipin 1 function is essential for developmen... | KEEP AS NON CORE | Summary: Inferred from the mouse ortholog: cell-autonomous lipin-1 is required for brown adipose tissue development/function (UCP1, PGC-1alpha, altered cold sensitivity). A genuine but tissue/physiology-level role that is downstream of lipin-1's lipid-metabolic and transcriptional functions; non-core. Supporting Evidence: PMID:23028044 Loss of lipin 1 also affected BAT development and function, as revealed by histological changes, defects in the expression of peroxisome proliferator-activated receptor alpha (PPARalpha), PGC-1alpha, and UCP1, and functionally by altered cold sensitivity. |
| GO:0005635 nuclear envelope | TAS Reactome:R-HSA-4419948 | KEEP AS NON CORE | Summary: Reactome localization for the nuclear-envelope pool where lipin-1 (PAP) is dephosphorylated by the CTDNEP1:CNEP1R1 complex. Real but non-core relative to the cytosol/ER catalytic pool. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt Dephosphorylated by the CTDNEP1-CNEP1R1 complex |
| GO:0005635 nuclear envelope | TAS Reactome:R-HSA-5195402 | KEEP AS NON CORE | Summary: Duplicate Reactome nuclear-envelope localization (CDK1 phosphorylates LPIN reaction context). Non-core, as above. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt Dephosphorylated by the CTDNEP1-CNEP1R1 complex |
| GO:0005635 nuclear envelope | TAS Reactome:R-HSA-5221130 | KEEP AS NON CORE | Summary: Duplicate Reactome nuclear-envelope localization tied to the PA-to-DAG conversion reaction. Non-core. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt Dephosphorylated by the CTDNEP1-CNEP1R1 complex |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4419948 | KEEP AS NON CORE | Summary: Reactome nucleoplasm localization, consistent with the nuclear pool of lipin-1 (transcriptional coregulation and regulated dephosphorylation). Non-core relative to the cytosol/ER catalytic pool. Supporting Evidence: PMID:11138012 The gene (Lpin1) encodes a novel nuclear protein which we have named lipin. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5195402 | KEEP AS NON CORE | Summary: Duplicate Reactome nucleoplasm localization. Non-core, as above. Supporting Evidence: PMID:11138012 The gene (Lpin1) encodes a novel nuclear protein which we have named lipin. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-1483203 | ACCEPT | Summary: Reactome ER-membrane localization for the "PA is dephosphorylated to DAG by LPIN" reaction. Core catalytic localization; ACCEPT (consistent with experimental ER annotation). Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt Endoplasmic reticulum membrane {ECO:0000269|PubMed:29765047}. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-75899 | ACCEPT | Summary: Duplicate Reactome ER-membrane localization tied to the DAG-3-phosphate hydrolysis reaction. Core catalytic localization; ACCEPT. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt Endoplasmic reticulum membrane {ECO:0000269|PubMed:29765047}. |
| GO:0005634 nucleus | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Nuclear localization inferred from the mouse ortholog; consistent with lipin-1's nuclear transcriptional-coregulator pool. Real but non-core. Supporting Evidence: PMID:11138012 The gene (Lpin1) encodes a novel nuclear protein which we have named lipin. |
| GO:0005737 cytoplasm | ISS GO_REF:0000024 | ACCEPT | Summary: Cytoplasmic localization inferred from the mouse ortholog; the resting lipin-1 pool is cytosolic. Correct but general; the more specific cytosol (GO:0005829) annotation is experimentally supported. ACCEPT as a core localization. Supporting Evidence: file:human/LPIN1/LPIN1-uniprot.txt Cytoplasm, cytosol {ECO:0000269|PubMed:29765047}. |
| GO:0006642 triglyceride mobilization | ISS GO_REF:0000024 | MARK AS OVER ANNOTATED | Summary: Inferred from the mouse ortholog. Lipin-1's direct enzymatic role is in triacylglycerol/glycerolipid biosynthesis (PA to DAG), not in mobilization (lipolysis) of stored triglyceride. Any influence on TAG mobilization is indirect (via transcriptional coactivation of lipid-oxidation genes); MARK_AS_OVER_ANNOTATED as a direct-involvement claim. |
| GO:0009062 fatty acid catabolic process | ISS GO_REF:0000024 | MARK AS OVER ANNOTATED | Summary: Duplicate of the IBA fatty-acid-catabolic-process annotation, here by ortholog transfer. Lipin-1's direct catalytic role is biosynthetic; the link to fatty acid catabolism is indirect via its transcriptional coactivation of fatty-acid-oxidation genes. Over-annotation as a direct-involvement claim. |
| GO:0005634 nucleus | ISS PMID:11138012 Lipodystrophy in the fld mouse results from mutation of a ne... | KEEP AS NON CORE | Summary: Nuclear localization based on the founding fld/lipin paper (which named lipin a nuclear protein) and mouse-ortholog inference. Real but non-core relative to the cytosol/ER catalytic pool. Duplicate of the other nucleus annotations. Supporting Evidence: PMID:11138012 The gene (Lpin1) encodes a novel nuclear protein which we have named lipin. |
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Download this section (compressed HTML)Q: Which lipin-1 splice isoforms and post-translational states (phosphorylation, acetylation, sumoylation) predominate in skeletal muscle, and how do they set the muscle rhabdomyolysis threshold in LPIN1 deficiency?
Q: How is the balance between lipin-1's cytosolic/ER PAP pool and its nuclear transcriptional-coregulator pool controlled in human cells, and is the nuclear transcriptional role independent of catalytic activity?
Experiment: Catalytically dead (DxDxT-motif) versus transcription-defective (LXXIL-motif) separation-of-function LPIN1 alleles in human myotubes/adipocytes to partition the PAP enzymatic and transcriptional-coactivator contributions to lipid homeostasis.
Experiment: Quantitative lipidomics (PA, DAG, TAG, PE, PC) after LPIN1 knockout/rescue in human cells to map the flux consequences of loss of lipin-1 PAP activity across the neutral-lipid and phospholipid branches.
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