Identification of structurally important domains of lipid phosphate phosphatase-1: implications for its sites of action

Zhang, Qiu‐Xia; Pilquil, Carlos; Dewald, Jay; Berthiaume, Luc G.; Brindley, David N.

doi:10.1042/0264-6021:3450181

Cited by 57 publications

(75 citation statements)

References 10 publications

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“…The topology of the S. cerevisiae LPP1 and DPP1 enzymes locates the phosphatase active site on the cytosolic side of the membranes [60]; therefore, changes in the enzyme levels may affect de novo phospholipid metabolism. This is in contrast to the mammalian LPP enzymes whose active sites are facing either the lumen of intracellular organelles or the exterior of the plasma membrane and, therefore, they are unlikely to participate in de novo biosynthesis [61][62][63].…”

Section: Phosphatidic Acid Phosphatasesmentioning

confidence: 95%

Comparative genomics and evolution of eukaryotic phospholipid biosynthesis

Lykidis

2007

Progress in Lipid Research

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Phospholipid biosynthetic enzymes produce diverse molecular structures and are often present in multiple forms encoded by different genes. This work utilizes comparative genomics and phylogenetics for exploring the distribution, structure and evolution of phospholipid biosynthetic genes and pathways in 26 eukaryotic genomes. Although the basic structure of the pathways was formed early in eukaryotic evolution, the emerging picture indicates that individual enzyme families followed unique evolutionary courses. For example, choline and ethanolamine kinases and cytidylyltransferases emerged in ancestral eukaryotes, whereas, multiple forms of the corresponding phosphatidyltransferases evolved mainly in a lineage specific manner.Furthermore, several unicellular eukaryotes maintain bacterial-type enzymes and reactions for the synthesis of phosphatidylglycerol and cardiolipin. Also, base-exchange phosphatidylserine synthases are widespread and ancestral enzymes. The multiplicity of phospholipid biosynthetic enzymes has been largely generated by gene expansion in a lineage specific manner. Thus, these observations suggest that phospholipid biosynthesis has been an actively evolving system. 2Finally, comparative genomic analysis indicates the existence of novel phosphatidyltransferases and provides a candidate for the uncharacterized eukaryotic phosphatidylglycerol phosphate phosphatase.

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Section: Phosphatidic Acid Phosphatasesmentioning

confidence: 95%

Comparative genomics and evolution of eukaryotic phospholipid biosynthesis

Lykidis

2007

Progress in Lipid Research

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“…However, three LPP domains are highly conserved in all Arabidopsis prokaryotic LPPs. Site-directed mutagenesis of these domains in yeast or mammalian LPP suggests that these domains are critical for enzymatic activity (25,26), and together they may form an active site because they all face the same side of the membrane in every case studied so far (27). However, using a deduced membrane topology of these LPPs that consider membrane-spanning regions, domain 3 of prokaryotic LPP in Arabidopsis faces the opposite side (predicted by SOSUI program, available at bp.nuap.nagoya-u.ac.jp/ sosui/).…”

Section: Discussionmentioning

confidence: 99%

“…The Newly Identified LPPs in Arabidopsis and Synechocystis Belong to a Distinct LPP Subgroup-The active sites of LPPs contain three conserved domains in which certain essential residues have been identified by site-directed mutagenesis (25,26). These domains are highly conserved among the newly identified LPP candidates in Synechocystis and Arabidopsis (Fig.…”

Section: A Strategy To Identify Plastidic Paps In Arabidopsis-mentioning

confidence: 99%

Plastidic Phosphatidic Acid Phosphatases Identified in a Distinct Subfamily of Lipid Phosphate Phosphatases with Prokaryotic Origin

Nakamura

Tsuchiya

Ohta

2007

Journal of Biological Chemistry

101

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Plastidic phosphatidic acid phosphatase (PAP) dephosphorylates phosphatidic acid to yield diacylglycerol, which is a precursor for galactolipids, a primary and indispensable component of photosynthetic membranes. Despite its functional importance, the molecular characteristics and phylogenetic origin of plastidic PAP were unknown because no potential homologs have been found. Here, we report the isolation and characterization of plastidic PAPs in Arabidopsis that belong to a distinct lipid phosphate phosphatase (LPP) subfamily with prokaryotic origin. Because no homolog of mammalian LPP was found in cyanobacteria, we sought an LPP ortholog in a more primitive organism, Chlorobium tepidum, and its homologs in cyanobacteria. Arabidopsis had five homologs of cyanobacterial LPP, three of which (LPP␥, LPP⑀1, and LPP⑀2) localized to chloroplasts. Complementation of yeast ⌬dpp1⌬lpp1⌬pah1 by plastidic LPPs rescued the relevant phenotype in vitro and in vivo, suggesting that they function as PAPs. Of the three LPPs, LPP␥ activity best resembled the native activity. The three plastidic LPPs were differentially expressed both in green and nongreen tissues, with LPP␥ expressed the highest in shoots. A knock-out mutant for LPP␥ could not be obtained, although a lpp⑀1lpp⑀2 double knock-out showed no significant changes in lipid composition. However, lpp␥ homozygous mutant was isolated only under ectopic overexpression of LPP␥, suggesting that loss of LPP␥ may cause lethal effect on plant viability. Thus, in Arabidopsis, there are three isoforms of plastidic PAP that belong to a distinct subfamily of LPP, and LPP␥ may be the primary plastidic PAP.

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“…We also employed fibroblasts obtained from transgenic mice that overexpressed 2 copies of the Lpp1 gene (24). Catalytically active LPP1 and the inactive R217K mutant (40) were transiently overexpressed by using adenoviral constructs at 40 multiplicity of infection for 24 h, when new serum-supplemented medium was added and the cells tested 18 h later (23). Knockdown of LPP1 activity was achieved using double-stranded SMARTpool® siRNAs designed to target rat LPP1 from Dharmacon Inc. (Lafayette, CO).…”

Section: Methodsmentioning

confidence: 99%

“…To investigate whether the effect of LPP1 on LPA-induced migration depends upon its catalytic activity, Rat2 fibroblasts were infected with adenoviral vectors containing mLPP1-myc or the inactive mLPP1(R217K)-myc (40). Overexpression of the wild-type LPP1 increased total LPP activity by about 4-fold, whereas expression of the mutant did not change LPP activity significantly (results not shown).…”

Section: Lpp1 Activity Regulates the Stimulation Of Fibroblast Migratmentioning

confidence: 99%

Lipid Phosphate Phosphatase-1 Regulates Lysophosphatidate-induced Fibroblast Migration by Controlling Phospholipase D2-dependent Phosphatidate Generation

Pilquil

Dewald

Cherney

et al. 2006

Journal of Biological Chemistry

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Identification of structurally important domains of lipid phosphate phosphatase-1: implications for its sites of action

Cited by 57 publications

References 10 publications

Comparative genomics and evolution of eukaryotic phospholipid biosynthesis

Comparative genomics and evolution of eukaryotic phospholipid biosynthesis

Plastidic Phosphatidic Acid Phosphatases Identified in a Distinct Subfamily of Lipid Phosphate Phosphatases with Prokaryotic Origin

Lipid Phosphate Phosphatase-1 Regulates Lysophosphatidate-induced Fibroblast Migration by Controlling Phospholipase D2-dependent Phosphatidate Generation

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