The discovery of the fat-regulating phosphatidic acid phosphatase gene

doi:10.1007/s11515-011-0910-7

Front Biol

2011, Vol. 6

Issue (3) : 172-176 https://doi.org/10.1007/s11515-011-0910-7

COMMENTARY

The discovery of the fat-regulating phosphatidic acid phosphatase gene

George M. CARMAN(

)

Department of Food Science and Rutgers Center for Lipid Research, Rutgers University, New Brunswick, New Jersey 08901, U.S.A.

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Abstract

Phosphatidic acid phosphatase is a fat-regulating enzyme that plays a major role in controlling the balance of phosphatidic acid (substrate) and diacylglycerol (product), which are lipid precursors used for the synthesis of membrane phospholipids and triacylglycerol. Phosphatidic acid is also a signaling molecule that triggers phospholipid synthesis gene expression, membrane expansion, secretion, and endocytosis. While this important enzyme has been known for several decades, its gene was only identified recently from yeast. This discovery showed the importance of phosphatidic acid phosphatase in lipid metabolism in yeast as well as in higher eukaryotes including humans.

Keywords phosphatidic acid phosphatase yeast lipin phospholipid triacylglycerol

Corresponding Author(s): CARMAN George M.,Email:carman@aesop.rutgers.edu

Issue Date: 01 June 2011

Cite this article:

George M. CARMAN. The discovery of the fat-regulating phosphatidic acid phosphatase gene[J]. Front Biol, 2011, 6(3): 172-176.

URL:

https://academic.hep.com.cn/fib/EN/10.1007/s11515-011-0910-7
https://academic.hep.com.cn/fib/EN/Y2011/V6/I3/172

Fig.1 The PA phosphatase reaction and its roles in lipid metabolism. The reaction catalyzed by PA phosphatase (highlighted in yellow) is shown. The reaction product diacylglycerol (DAG) is used for the synthesis of triacylglycerol (TAG) and the synthesis of phosphatidylethanolamine (PE) or phosphatidylcholine (PC). The reaction substrate PA is used for the synthesis of phosphatidylinositol (PI) or phosphatidylglycerol (PG) via CDP-diacylglycerol (CDP-DAG). The substrate and product of the PA phosphatase reaction also play roles in lipid signaling.

Fig.2 Domain structures of the yeast and human PAP enzymes. The diagram shows the positions of the conserved NLIP () and HAD-like () domains in yeast PAP and human lipin 1. These domains are conserved in lipin 2 and lipin 3 (not shown). A conserved glycine residue within the NLIP domain and conserved aspartate residues in the catalytic sequence DIDGT within the HAD-like domain are essential for PAP activity.

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