Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The phosphatidic acid-binding, polybasic domain is responsible for the differences in the phosphoregulation of lipins 1 and 3.

The Journal of biological chemistry - 15 Dec 2017

Boroda Salome, Takkellapati Sankeerth, Lawrence Robert T, Entwisle Samuel W, Pearson Jennifer M, Granade Mitchell E, Mullins Garrett R, Eaton James M, Villén Judit, Harris Thurl E

Abstract excerpt

Lipins 1, 2, and 3 are Mg2+-dependent phosphatidic acid phosphatases and catalyze the penultimate step of triacylglycerol synthesis. We have previously investigated the biochemistry of lipins 1 and 2 and shown that di-anionic phosphatidic acid (PA) augments their activity and lipid binding and that lipin 1 activity is negatively regulated by phosphorylation. In the present study, we show that phosphorylation does...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to 3T3-L1 Cells
Share to Conserved Sequence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Liposomes

Share to Micelles

Share to Phosphatidate Phosphatase

Share to Phosphatidic Acids

Share to Protein Interaction Domains and Motifs

Share to Protein Processing, Post-Translational

Source

Open in PubMed Open full text

Identifiers

PMID: 28982975
DOI: 10.1074/jbc.M117.786574
PMCID: PMC5733587

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The phosphatidic acid-binding, polybasic domain is responsible for the differences in the phosphoregulation of lipins 1 and 3.PMID 28982975Read ↗

Lipin proteins form homo- and hetero-oligomers.Semantic proximity Read ↗

Thematic Review Series: Glycerolipids. Multiple roles for lipins/phosphatidate phosphatase enzymes in lipid metabolism.Semantic proximity Read ↗

Roles of phosphatidate phosphatase enzymes in lipid metabolism.Semantic proximity Read ↗

Lipin proteins and glycerolipid metabolism: Roles at the ER membrane and beyond.Semantic proximity Read ↗

Lipins: multifunctional lipid metabolism proteins.Semantic proximity Read ↗

Structural determinants for phosphatidic acid regulation of phospholipase C-beta1.Semantic proximity Read ↗

The cellular functions of the yeast lipin homolog PAH1p are dependent on its phosphatidate phosphatase activity.Semantic proximity Read ↗

Phosphatidate phosphatase-1 is functionally conserved in lipid synthesis and storage from human to yeast.Semantic proximity Read ↗

Identification of diverse lipid droplet targeting motifs in the PNPLA family of triglyceride lipases.Semantic proximity Read ↗

Mice with an adipocyte-specific lipin 1 separation-of-function allele reveal unexpected roles for phosphatidic acid in metabolic regulation.Semantic proximity Read ↗

Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, lipin 1.Semantic proximity Read ↗

Identification of a novel phosphatidic acid binding domain in protein phosphatase-1.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.