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Review
. 2009 Jan 30;284(5):2593-7.
doi: 10.1074/jbc.R800059200. Epub 2008 Sep 23.

Phosphatidic acid phosphatase, a key enzyme in the regulation of lipid synthesis

George M Carman  1 , Gil-Soo Han
Affiliations
Review

Phosphatidic acid phosphatase, a key enzyme in the regulation of lipid synthesis

George M Carman et al. J Biol Chem. .
No abstract available

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Figures

FIGURE 1.
FIGURE 1.
Roles of PAP in lipid synthesis and signaling in yeast. The reaction catalyzed by PAH1-encoded PAP (highlighted in yellow) is shown. Regulation of PAP activity plays a role in governing whether cells synthesize membrane phospholipids via CDP-DAG or DAG. The reaction product DAG is also used for the synthesis of the storage lipid TAG. The substrate PA signals growth of the nuclear/ER membrane and the transcriptional regulation of UASINO-containing phospholipid synthesis genes. The signaling roles of PAP are counteracted by the activity of DGK1-encoded DAG kinase (DGK). In mammalian cells, phosphatidylserine (PS), PE, and PC are derived from DAG, and DAG kinase uses ATP instead of CTP as the phosphate donor in its reaction (54, 55). PG, phosphatidylglycerol.
FIGURE 2.
FIGURE 2.
Domain structures and phosphorylation sites of the yeast and mouse PAP enzymes. The diagram shows the positions of the NLIP (blue) and HAD-like (yellow) domains in yeast PAP and mouse lipin 1β. These domains are conserved in lipins 1α, 2, and 3 (not shown) (16). The conserved glycine residue within the NLIP domain and the conserved aspartate residues in the catalytic sequence DIDGT within the HAD-like domain are essential for PAP activity (15, 30, 53). The positions of the phosphorylation sites identified in the yeast (21) and mouse (53) enzymes are indicated. The sites shown on the upper portion of the yeast PAP diagram are targets for Cdk1 phosphorylation (21).
See this image and copyright information in PMC

References

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