F
IPR043216

Phosphatidate (PA) phosphatase-related

InterPro entry
Short namePA_PP_rel
Overlapping
homologous
superfamilies
 

Description

This entry represents a group of membrane-associated phosphatidic acid phosphatases and their homologues mostly found in metazoa, fungi and plants.

In budding yeasts there are two members, Lpp1 and Dpp1. Lpp1 catalyzes the Mg(2+)-independent dephosphorylation of phosphatidate (PA), diacylglycerol pyrophosphate (DGPP), and lysophosphatidate (LPA)
[4]
. Dpp1, a zinc-regulated enzyme that catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG)
[1]
.

In humans, the members are phospholipid phosphatase 1-5 (PLPP1-5) and phospholipid phosphatase-related protein type 1-5 (PLPR1-5). PLPPs are magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters
[5, 6, 7]
. PLPR1-5 may not have 2-lysophosphatidate/LPA phosphatase activity due to the lacking of critical residues supporting the reaction mechanism in active phosphatases of this phosphoesterase family.

Plant members of this group are constitutively expressed in many tissues and exhibit both diacylglycerol pyrophosphate phosphatase activity as well as phosphatidate (PA) phosphatase activity
[3]
. Another lipid phosphate phosphatase (LPP) homologue, Wunen, is a drosophila protein expressed in the central nervous system, which provides repellent activity towards primordial germ cells (PGCs), controls the survival of PGCs and is essential in the migration process of these cells towards the somatic gonadal precursors
[2]
.

References

1.Regulation of the Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase by zinc. Han GS, Johnston CN, Chen X, Athenstaedt K, Daum G, Carman GM. J Biol Chem 276, 10126-33, (2001). PMID: 11139591

2.Fly and mammalian lipid phosphate phosphatase isoforms differ in activity both in vitro and in vivo. Burnett C, Howard K. EMBO Rep 4, 793-9, (2003). PMID: 12856002

3.Lipid phosphate phosphatases in Arabidopsis. Regulation of the AtLPP1 gene in response to stress. Pierrugues O, Brutesco C, Oshiro J, Gouy M, Deveaux Y, Carman GM, Thuriaux P, Kazmaier M. J. Biol. Chem. 276, 20300-8, (2001). View articlePMID: 11278556

4.Enzymological properties of the LPP1-encoded lipid phosphatase from Saccharomyces cerevisiae. Furneisen JM, Carman GM. Biochim Biophys Acta 1484, 71-82, (2000). PMID: 10685032

5.Lipid phosphate phosphohydrolase-1 degrades exogenous glycerolipid and sphingolipid phosphate esters. Jasinska R, Zhang QX, Pilquil C, Singh I, Xu J, Dewald J, Dillon DA, Berthiaume LG, Carman GM, Waggoner DW, Brindley DN. Biochem J 340 ( Pt 3), 677-86, (1999). PMID: 10359651

6.Lipid phosphate phosphatase-2 activity regulates S-phase entry of the cell cycle in Rat2 fibroblasts. Morris KE, Schang LM, Brindley DN. J Biol Chem 281, 9297-306, (2006). PMID: 16467304

7.Cloning and characterization of DPPL1 and DPPL2, representatives of a novel type of mammalian phosphatidate phosphatase. Takeuchi M, Harigai M, Momohara S, Ball E, Abe J, Furuichi K, Kamatani N. Gene 399, 174-80, (2007). View articlePMID: 17590538

Further reading

8. Current views on regulation and function of plasticity-related genes (PRGs/LPPRs) in the brain. Strauss U, Brauer AU. Biochim. Biophys. Acta 1831, 133-8, (2013). View articlePMID: 23388400

9. Cooperative interactions of LPPR family members in membrane localization and alteration of cellular morphology. Yu P, Agbaegbu C, Malide DA, Wu X, Katagiri Y, Hammer JA, Geller HM. J. Cell. Sci. 128, 3210-22, (2015). View articlePMID: 26183180

GO terms

molecular function

  • None

cellular component

  • None

Cross References

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