ArticleThe Journal of biological chemistry2014
Lipin 2 binds phosphatidic acid by the electrostatic hydrogen bond switch mechanism independent of phosphorylation.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 35 citations in OpenAlex.
- Bacterial cell fate under stress: lipid remodeling and antimicrobial peptide attack.npj antimicrobials and resistance · 2026Article
- A fluorescence and HPLC-based activity assay system for lipid-modifying enzymes: Lipin/Pah phosphatidic acid phosphatase as an optimized example.Methods in enzymology · 2026Article
- Lipin phosphatidic acid phosphatases: Structure, function, regulation, and disease association.Advances in biological regulation · 2025Review
- Architecture and function of yeast phosphatidate phosphatase Pah1 domains/regions.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024Review
- Article
- Role of lipins in cardiovascular diseases.Lipids in health and disease · 2023Review
- Article
- Selectivity of mTOR-Phosphatidic Acid Interactions Is Driven by Acyl Chain Structure and Cholesterol.Cells · 2021Article
- The middle lipin domain adopts a membrane-binding dimeric protein fold.Nature communications · 2021Article
- Crystal structure of a lipin/Pah phosphatidic acid phosphatase.Nature communications · 2020Article
- Article
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- Mammalian lipin phosphatidic acid phosphatases in lipid synthesis and beyond: metabolic and inflammatory disorders.Journal of lipid research · 2019Review
- Host phosphatidic acid phosphatase lipin1 is rate limiting for functional hepatitis C virus replicase complex formation.PLoS pathogens · 2018Article
- The phosphatidic acid-binding, polybasic domain is responsible for the differences in the phosphoregulation of lipins 1 and 3.The Journal of biological chemistry · 2017Article
- The ins and outs of endoplasmic reticulum-controlled lipid biosynthesis.EMBO reports · 2017Review
- How lipid droplets "TAG" along: Glycerolipid synthetic enzymes and lipid storage.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- Lipin proteins and glycerolipid metabolism: Roles at the ER membrane and beyond.Biochimica et biophysica acta. Biomembranes · 2017Review
- Chronic Recurrent Multifocal Osteomyelitis and Related Diseases-Update on Pathogenesis.Current rheumatology reports · 2017Review
- Lipid partitioning at the nuclear envelope controls membrane biogenesis.Molecular biology of the cell · 2015Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Lipin 2 is a phosphatidic acid phosphatase (PAP) responsible for the penultimate step of triglyceride synthesis and dephosphorylation of phosphatidic acid (PA) to generate diacylglycerol. The lipin family of PA phosphatases is composed of lipins 1-3, which are members of the conserved haloacid dehalogenase superfamily. Although genetic alteration of LPIN2 in humans is known to cause Majeed syndrome, little is known about the biochemical regulation of its PAP activity. Here, in an attempt to gain a better general understanding of the biochemical nature of lipin 2, we have performed kinetic and phosphorylation analyses. We provide evidence that lipin 2, like lipin 1, binds PA via the electrostatic hydrogen bond switch mechanism but has a lower rate of catalysis. Like lipin 1, lipin 2 is highly phosphorylated, and we identified 15 phosphosites. However, unlike lipin 1, the phosphorylation of lipin 2 is not induced by insulin signaling nor is it sensitive to inhibition of the mammalian target of rapamycin. Importantly, phosphorylation of lipin 2 does not negatively regulate either membrane binding or PAP activity. This suggests that lipin 2 functions as a constitutively active PA phosphatase in stark contrast to the high degree of phosphorylation-mediated regulation of lipin 1. This knowledge of lipin 2 regulation is important for a deeper understanding of how the lipin family functions with respect to lipid synthesis and, more generally, as an example of how the membrane environment around PA can influence its effector proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.