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Biomolecular Concepts

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Volume 4, Issue 5


Plant phospholipase A: advances in molecular biology, biochemistry, and cellular function

Guanqun Chen
  • Alberta Innovates Phytola Centre, Department of Agricultural, Food and Nutritional Science, 410 Agriculture/Forestry Centre, University of Alberta, Edmonton, Alberta, Canada T6G 2P5
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Michael S. Greer
  • Alberta Innovates Phytola Centre, Department of Agricultural, Food and Nutritional Science, 410 Agriculture/Forestry Centre, University of Alberta, Edmonton, Alberta, Canada T6G 2P5
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  • De Gruyter OnlineGoogle Scholar
/ Randall J. Weselake
  • Corresponding author
  • Alberta Innovates Phytola Centre, Department of Agricultural, Food and Nutritional Science, 410 Agriculture/Forestry Centre, University of Alberta, Edmonton, Alberta, Canada T6G 2P5
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  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2013-07-23 | DOI: https://doi.org/10.1515/bmc-2013-0011


Plant phospholipase As (PLAs) are a complex group of enzymes that catalyze the release of free fatty acids from phospholipids. Plant PLAs can be grouped into three families, PLA1, PLA2, and patatin-like PLA, that catalyze the hydrolysis of acyl groups from the sn-1 and/or sn-2 position. Each family is composed of multiple isoforms of phospholipases that differ in structural, catalytic, and physiological characteristics. In this review, recently acquired information on molecular, biochemical, and functional aspects of plant PLAs will be discussed.

Keywords: lipid biosynthesis; phospholipase; plant development; signal transduction; stress response


Enzymes of the phospholipase A (PLA) family catalyze the hydrolysis of acyl groups from phospholipids to produce free fatty acids and lysophospholipids. PLAs represent one of the earliest enzymes to be characterized, which traces back to the identification of lytic actions of snake venom at the end of the 19th century (1). Plants possess a complex and diverse set of PLA enzymes that differ in nucleotide sequence, protein structure, enzymatic properties, cellular functions, and anthropocentric applications (2–7). Here, we review the functions of plant PLAs, with particular focus on information acquired in the past 3 years.

Plant PLA genes and proteins

Defined by the bond that they work on, plants have three families of PLAs. PLA1 and PLA2 enzymes catalyze the hydrolysis of acyl groups from the sn-1 and sn-2 position, respectively, and patatin-like PLAs (pPLAs) exhibit activity toward both positions (Figure 1). It should be noted that this generally accepted classification system is convenient, but is neither very accurate nor broad enough to cover all enzymes with PLA activity. For instance, oleosin has recently been shown to be a bifunctional enzyme with both monoacylglycerol acyltransferase and PLA activities (8). Also, a lecithin:cholesterol acyltransferase (LCAT)-like PLA, which is not a pPLA, shows both PLA1 and PLA2 activities, with a preference for acyl groups at the sn-2 position (9). In this review, this LCAT-PLA will be included in the discussion of the PLA1 family, as it is the closest homologue of LCAT-PLA1. Oleosin and other multifunctional enzymes with PLA activities will not be included in this review.

Positional specificity of plant phospholipase As (PLAs) on phospholipids. FA, fatty acyl chain; pPLA, patatin-like PLA. Some plant PLAs can also use glycolipids, lysophospholipids, and neutral glycerolipids as substrates (Table 1).
Figure 1

Positional specificity of plant phospholipase As (PLAs) on phospholipids. FA, fatty acyl chain; pPLA, patatin-like PLA. Some plant PLAs can also use glycolipids, lysophospholipids, and neutral glycerolipids as substrates (Table 1).

Fourteen genes encoding PLA1s have been identified in Arabidopsis, which can be divided into five classes based on the presence of particular N-terminal stretches and sequence similarities in the catalytic region (Table 1). All known plant PLA1s have molecular masses of 45–50 kDa, contain a conserved GXSXG motif, and have a catalytic triad composed of a serine, an aspartic acid, and a histidine residue (3). In contrast, their cellular localizations are diverse (4, 10–12). AtPLA1-Iα1 is localized to cytoplasmatic lipid bodies that are often associated with chloroplasts, whereas the other six class I PLA1s are targeted to plastids (10–14). All four class II PLA1s are predicted to be localized to the cytosol, which has been demonstrated experimentally for AtPLA1-IIγ and AtPLA1-IIδ (4, 15, 16). AtPLA1-III and AtPA-PLA1 are localized to the mitochondria and vacuolar membranes, respectively (17, 18). The transcription of PLA1 genes can be diverse as well. PLA1 transcripts can generally be detected in almost all plant organs, but the individual isoforms vary considerably in their temporal or tissue specificity (11–15, 19). For example, AtPLA1-III is highly expressed in seedlings. The carnation PLA1-II is expressed in 4- to 5-day-old roots, whereas LCAT-PLA is expressed in both roots and developing siliques (9, 17, 19).

Table 1

Arabidopsis phospholipases (AtPLAs).

Plants have a relatively much simpler and less complex pool of ‘real’ PLA2s (phospholipases that have only PLA2 activity but no PLA1 activity) compared with plant PLA1s, and those from animals and other sources. Only four soluble PLA2s have been identified in Arabidopsis (AtPLA2-α, -β, -γ, and -δ) (6). Similar to animal secretory PLA2s (sPLA2s), all four of these PLA2s have low molecular masses of 13–18 kDa. All of these plant sPLA2s also contain a catalytic site DACCxxHDxC motif with a well-conserved histidine-aspartate dyad, and a calcium-binding loop (YGKYCGxxxxGC) (20). Regarding protein localization, AtPLA2-α is localized to the Golgi, AtPLA2-β and AtPLA2-δ are localized to the endoplasmic reticulum, and AtPLA2-γ is localized to both the endoplasmic reticulum and the Golgi (21–23). A recent study indicates that AtPLA2-α can also be localized to the nucleus in the presence of AtMYB30 (24). The transcripts of AtsPLA2s are tissue specific: sPLA2-α is expressed in most tissues with the exception of siliques; the expression of sPLA2-β can be detected in flowers and siliques but not in maturing seeds; sPLA2-δ and -γ are only expressed in floral tissues (20, 25, 26). Recently, Kim et al. (23) used RT-PCR to compare the expression profiles of all four AtsPLA2s in pollen. AtsPLA2, , and -δ, but not AtsPLA2-α, were expressed in pollen, potentially indicating an important role for class II but not class I sPLA2s in pollen development. Environmental conditions can also affect sPLA2 expression. For example, the expression of Citrus sinensis sPLA2 and sPLA2 exhibited diurnal rhythmicity in leaf and fruit tissues, suggesting accompanying daily cycle changes in second messengers (27).

Patatins are a group of vacuolar non-specific lipid hydrolases in tubers of solanaceous plants with combined PLA1, PLA2, and galactolipase activities. Arabidopsis has 10 pPLA enzymes that can be divided into three classes based on their genomic sequences (Table 1). AtpPLA-I has a molecular mass of 156 kDa, which is much larger than the other AtpPLAs (averaging 45 kDa) (28). Class I and II pPLAs have a catalytic dyad, composed of a typical serine hydrolase motif of GXSXG, and a conserved aspartic acid within a patatin domain. The class III pPLAs, conversely, have a hydrolase motif sequence of GXGXG (5, 29, 30). The localizations of the six AtpPLAs have all been identified. AtpPLA-I is localized in the chloroplasts; pPLA-IIδ, ɛ, and γ are localized to the cytoplasm and associate with membranes such as plasma or endoplasmic reticulum membrane. pPLA-IIIβ associates with the plasma membrane, and pPLA-IIIδ is localized to both the plasma and intracellular membranes (28, 29, 31, 32). Similar to sPLA2s, pPLAs have a range of expression profiles among different plant tissues (Table 1). For instance, AtpPLA-IIγ is expressed preferentially in flowers and siliques, but AtpPLA-IIe is mainly expressed in roots (28). AtpPLA-IIIα has the highest expression level in siliques, whereas the other three AtpPLA-IIIs are expressed predominantly in roots (31).

Enzymatic properties of plant PLAs

The enzymatic properties of several plant PLAs have been studied through recombinant expression in yeast or Escherichia coli. These enzymes exhibit a broad range of calcium dependencies, substrate specificities, and pH and temperature optimums.

In general, all the characterized PLA1s are calcium independent, can use phosphatidylcholine (PC) as substrate, and prefer a pH in the range of 5.0–7.5. Individual PLA1s, however, exhibit different catalytic properties. For instance, all AtPLA1-Is and AtPLA1-III can use monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG), and triacylglycerol (TAG) as substrates in addition to PC; however, AtLCAT-PLA1 cannot catalyze the hydrolysis of non-phospholipid substrates (11, 17, 33). AtLCAT-PLA, a homologue of animal lysosomal PLA2 (group XV), can use phospholipids but not lysophospholipids as substrates (9, 34).

The catalytic properties of the four AtsPLA2s have been extensively characterized. As shown in Table 1, AtsPLA2-α, -β, -δ, and -γ are all calcium dependent and can use PC and phosphatidylethanolamine (PE) as substrate; however, their optimal pH vary from 8.5 to 9.0, 6.0 to 7.0, 7.0 to 9.0, and 8.0 to 9.0, respectively (20, 35). Recently, sPLA2s have also been characterized in other plants, including tobacco, soybean, and wheat (36–38). Interestingly, a purified tobacco class II sPLA2, Nt1-PLA2, showed both PLA1 and PLA2 activities (37). The authors used non-radiolabeled substrates in their enzyme assays, and then labeled the released fatty acids with 9-anthryldiazomethane for high-performance liquid chromatography analysis. As PLA1 activity has never been reported for other plant sPLA2s, it would be interesting to verify this result directly using radiolabeled substrates.

All three classes of pPLAs are capable of catalyzing the hydrolysis of phospholipids and other glycerolipids at both the sn-1 and sn-2 positions (3, 5, 29). AtpPLA-I, the only class I pPLA, preferentially catalyzes the hydrolysis of phosphatidic acid (PA) and phosphatidylserine (PS) at the sn-2 position, and phosphatidylinositol (PI), PC, PE, and phosphatidylglycerol (PG) at the sn-1 position. Furthermore, AtpPLA-I catalyzes the hydrolysis of MGDG four times faster than PG (39). Surveying class II pPLAs, AtpPLA-IIα showed strong PLA1 activity toward PC and PE; strong PLA2 activity toward PG, PI, PA, and PS; and strong hydroxylase activity toward other membrane glycolipids, including MGDG, DGDG, and even oxidized glycolipids (30). AtpPLA-IIγ, -IIɛ, and -IIδ can act on glycolipids and phospholipids, but not on TAG (40). To describe class III pPLAs, AtpPLA-IIIβ can catalyze the hydrolysis of phospholipids and glycolipids but not neutral lipids, and PA is the preferred substrate. AtpPLA-IIIδ has five times greater PLA2 activity than PLA1 activity when PC is used as a substrate. Although its activity toward other lipid classes has not been described, it would not be surprising if this enzyme could catalyze the hydrolysis of glycolipids and other phospholipids. Interestingly, both AtpPLA-IIIβ and -IIIδ have thioesterase activity (29, 31).

Biological roles of plant PLAs

PLAs are involved in a wide range of cellular processes, many of which are believed to be linked to the accumulation of free fatty acids and lysophospholipids as either signaling molecules or building blocks in lipid metabolism (3, 4, 41). Here, we summarize the physiological aspects of plant PLAs with a focus on their recently identified roles (Table 1). Although some animal PLAs also have functions in signaling transduction and lipid metabolism, we cannot find similar biological roles of plant PLAs and their animal counterparts [for the functions of animal PLAs, please see ref. (42)].

During the past decade, substantial advances have been made toward understanding the biological functions of plant PLA1s. Among class I PLA1s, AtPLA1-Iα1, AtPLA1-Iβ1, and AtPLA1-Iγ1 are important for jasmonic acid production (10, 12, 13). Class II PLA1s have numerous important roles, including ultraviolet B-induced defense signaling (AtPLA1-IIδ), onset of senescence (Dianthus caryophyllus PLA1-IIδ), seedling establishment (AtPLA1-IIγ), and also cell development and tissue growth (Capsicum annuum PLA1-IIγ) (15, 19, 43). The sole class III AtPLA1, AtPLA1-III, plays an important role in seed viability and longevity. Also, AtPLA1-III-overexpressing lines possess significantly longer roots than the atpla1-iii knockout or wild-type seedlings. Also, AtPLA1-III may help protect and/or maintain seed contents that are important for germination, as AtPLA1-III-overexpressing seeds showed a strong tolerance to accelerated-aging treatments (17). Regarding other PLA1s, AtPA-PLA1 plays an important role in the early phases of shoot gravitropism (44). Although the enzymatic properties of AtLCAT-PLA1 and AtLCAT-PLA have been reported, their functions in plants remain to be explored (9, 33).

Compared with other plant PLAs, sPLA2s have been most extensively studied. To date, sPLA2 enzymes have been shown to be involved in numerous developmental processes (4, 21, 22, 24, 26). For example, AtsPLA2-α is required for the trafficking of PIN-FORMED proteins (auxin efflux transporters) to the plasma membrane, and may negatively regulate AtMYB30-mediated pathogen defense (22, 24). AtsPLA2-β produces second messengers to enhance light-induced stomatal opening and also contributes to cell elongation and shoot gravitropism through the auxin signaling pathway (21, 26, 45). Additionally, all three class II sPLA2s play critical roles in pollen development and pollen tube growth, most likely by modulating membrane deformation and enabling membrane trafficking (23).

Recent studies with transgenic plants indicate that the 10 plant pPLAs have unique yet overlapping functions. AtpPLA-I contributes to basal, but not pathogen- or wound-induced jasmonic acid production (39). Class II pPLAs modulate oxylipin formation (AtpPLA-IIα), water loss (AtpPLA-IIα), root development (AtpPLA-IIγ and AtpPLA-IIɛ), and stress responses (AtpPLA-IIα, AtpPLA-IIα, and AtpPLA-IIγ) (30, 40, 46–48). None of these pPLAs, however, are involved in providing free fatty acids for jasmonic acid biosynthesis (39). Among class III pPLAs, AtpPLA-IIIβ was found to be involved in cell elongation, cellulose accumulation, and lipid metabolism (31). In T-DNA insertional knockout mutants of the four pPLA-IIIs, only the ppla-iiiδ knockout mutant seeds had significantly lower oil contents. Conversely, when pPLA-IIIδ was overexpressed in Arabidopsis, the mutant had increased TAG content, without detrimental effect on overall seed yield per plant (29). As AtpPLA-IIIβ and AtpPLA-IIIδ have been reported to be involved in seed acyl lipid biosynthesis, further functional studies of lipid-hydrolyzing enzymes from other plants, particularly class III pPLAs, could better our understanding of lipid metabolism.

Conclusions and perspectives

Our understanding of plant PLAs has increased substantially over the past decade. A comprehensive and complex collection of PLAs have been identified, and further shown to exhibit a broad range of catalytic properties and biological functions. Some important questions, however, still remain. Further studies are necessary to elucidate the precise role(s) of each individual PLA in the phospholipid signaling networks, the upstream and downstream targets of lipid products generated by plant PLAs, and the functions of PLAs in lipid metabolism.

This work is part of the European Commission Seventh Framework Programme-sponsored project: Industrial Crops producing value Oils for Novel chemicals (ICON). RJW is grateful for the support provided by AVAC Ltd., Alberta Enterprise and Advanced Education, Alberta Innovates Bio Solutions, the Canada Foundation for Innovation, and the Canada Research Chairs Program.


  • 1.

    Stephens JWW, Myers W. The action of cobra poison on the blood: a contribution to the study of passive immunity. J Pathol Bacteriol 1898; 5: 279–301.CrossrefGoogle Scholar

  • 2.

    Wang X. Plant phospholipases. Annu Rev Plant Physiol Plant Mol Biol 2001; 52: 211–31.CrossrefPubMedGoogle Scholar

  • 3.

    Chen G, Snyder CL, Greer MS, Weselake RJ. Biology and biochemistry of plant phospholipases. Crit Rev Plant Sci 2011; 30: 239–58.CrossrefWeb of ScienceGoogle Scholar

  • 4.

    Ryu SB. Phospholipid-derived signaling mediated by phospholipase A in plants. Trends Plant Sci 2004; 9: 229–35.CrossrefWeb of SciencePubMedGoogle Scholar

  • 5.

    Scherer GFE, Ryu SB, Wang XM, Matos AR, Heitz T. Patatin-related phospholipase A: nomenclature, subfamilies and functions in plants. Trends Plant Sci 2010; 15: 693–700.PubMedCrossrefWeb of ScienceGoogle Scholar

  • 6.

    Wang G, Ryu S, Wang X. Plant phospholipases: an overview. Methods Mol Biol 2012; 861: 123–37.Web of ScienceGoogle Scholar

  • 7.

    Casado V, Martin D, Torres C, Reglero G. Phospholipases in food industry: a review. Methods Mol Biol 2012; 861: 495–523.Web of ScienceGoogle Scholar

  • 8.

    Parthibane V, Rajakumari S, Venkateshwari V, Iyappan R, Rajasekharan R. Oleosin is bifunctional enzyme that has both monoacylglycerol acyltransferase and phospholipase activities. J Biol Chem 2012; 287: 1946–54.Web of ScienceGoogle Scholar

  • 9.

    Chen G, Greer MS, Lager I, Yilmaz JL, Mietkiewska E, Carlsson AS, Stymne S, Weselake RJ. Identification and characterization of an LCAT-like Arabidopsis thaliana gene encoding a novel phospholipase A. FEBS Lett 2012; 586: 373–7.Web of ScienceGoogle Scholar

  • 10.

    Ellinger D, Stingl N, Kubigsteltig II, Bals T, Juenger M, Pollmann S, Berger S, Schuenemann D, Mueller MJ. Dongle and defective in anther Dehiscence1 lipases are not essential for wound- and pathogen-induced jasmonate biosynthesis: redundant lipases contribute to jasmonate formation. Plant Physiol 2010; 153: 114–27.Web of ScienceGoogle Scholar

  • 11.

    Seo YS, Kim EY, Kim JH, Kim WT. Enzymatic characterization of class I DAD1-like acyl hydrolase members targeted to chloroplast in Arabidopsis. FEBS Lett 2009; 583: 2301–7.Web of ScienceGoogle Scholar

  • 12.

    Hyun Y, Choi S, Hwang HJ, Yu J, Nam SJ, Ko J, Park JY, Seo YS, Kim EY, Ryu SB, Kim WT, Lee YH, Kang H, Lee I. Cooperation and functional diversification of two closely related galactolipase genes for jasmonate biosynthesis. Dev Cell 2008; 14: 183–92.PubMedCrossrefWeb of ScienceGoogle Scholar

  • 13.

    Ishiguro S, Kawai-Oda A, Ueda J, Nishida I, Okada K. The defective in anther dehiscence1 gene encodes a novel phospholipase A1 catalyzing the initial step of jasmonic acid biosynthesis, which synchronizes pollen maturation, anther dehiscence, and flower opening in Arabidopsis. Plant Cell 2001; 13: 2191–209.PubMedCrossrefGoogle Scholar

  • 14.

    Padham AK, Hopkins MT, Wang TW, McNamara LM, Lo M, Richardson LGL, Smith MD, Taylor CA, Thompson JE. Characterization of a plastid triacylglycerol lipase from Arabidopsis. Plant Physiol 2007; 143: 1372–84.CrossrefPubMedGoogle Scholar

  • 15.

    Lo M, Taylor C, Wang L, Nowack L, Wang TW, Thompson J. Characterization of an ultraviolet B-induced lipase in Arabidopsis. Plant Physiol 2004; 135: 947–58.Google Scholar

  • 16.

    Kim EY, Seo YS, Kim WT. AtDSEL, an Arabidopsis cytosolic DAD1-like acylhydrolase, is involved in negative regulation of storage oil mobilization during seedling establishment. J Plant Physiol 2011; 168: 1705–9.Web of ScienceGoogle Scholar

  • 17.

    Seo YS, Kim EY, Kim WT. The Arabidopsis sn-1-specific mitochondrial acylhydrolase AtDLAH is positively correlated with seed viability. J Exp Bot 2011; 62: 5683–98.Web of SciencePubMedCrossrefGoogle Scholar

  • 18.

    Morita MT, Kato T, Nagafusa K, Saito C, Ueda T, Nakano A, Tasaka M. Involvement of the vacuoles of the endodermis in the early process of shoot gravitropism in Arabidopsis. Plant Cell 2002; 14: 47–56.CrossrefPubMedGoogle Scholar

  • 19.

    Seo YS, Kim EY, Mang HG, Kim WT. Heterologous expression, and biochemical and cellular characterization of CaPLA1 encoding a hot pepper phospholipase A1 homolog. Plant J 2008; 53: 895–908.Web of ScienceGoogle Scholar

  • 20.

    Lee HY, Bahn SC, Shin JS, Hwang I, Back K, Doelling JH, Ryu SB. Multiple forms of secretory phospholipase A2 in plants. Prog Lipid Res 2005; 44: 52–67.PubMedCrossrefGoogle Scholar

  • 21.

    Seo J, Lee HY, Choi H, Choi Y, Lee Y, Kim YW, Ryu SB. Phospholipase A2-b mediates light-induced stomatal opening in Arabidopsis. J Exp Bot 2008; 59: 3587–94.CrossrefWeb of ScienceGoogle Scholar

  • 22.

    Lee OR, Kim SJ, Kim HJ, Hong JK, Ryu SB, Lee SH, Ganguly A, Cho HT. Phospholipase A2 is required for PIN-FORMED protein trafficking to the plasma membrane in the Arabidopsis root. Plant Cell 2010; 22: 1812–25.CrossrefPubMedGoogle Scholar

  • 23.

    Kim HJ, Ok SH, Bahn SC, Jang J, Oh SA, Park SK, Twell D, Ryu SB, Shin JS. Endoplasmic reticulum- and Golgi-localized phospholipase A2 plays critical roles in Arabidopsis pollen development and germination. Plant Cell 2011; 23: 94–110.CrossrefPubMedGoogle Scholar

  • 24.

    Froidure S, Canonne J, Daniel X, Jauneau A, Briere C, Roby D, Rivas S. AtsPLA2-α nuclear relocalization by the Arabidopsis transcription factor AtMYB30 leads to repression of the plant defense response. Proc Natl Acad Sci USA 2010; 107: 15281–6.Google Scholar

  • 25.

    Ryu SB, Lee HY, Doelling JH, Palta JP. Characterization of a cDNA encoding Arabidopsis secretory phospholipase A2-α, an enzyme that generates bioactive lysophospholipids and free fatty acids. BBA – Mol Cell Biol L 2005; 1736: 144–51.Google Scholar

  • 26.

    Lee HY, Bahn SC, Kang Y-M, Lee KH, Kim HJ, Noh EK, Palta JP, Shin JS, Ryu SB. Secretory low molecular weight phospholipase A2 plays important roles in cell elongation and shoot gravitropism in Arabidopsis. Plant Cell 2003; 15: 1990–2002.PubMedCrossrefGoogle Scholar

  • 27.

    Liao HL, Burns JK. Light controls phospholipase A2-α and -β gene expression in Citrus sinensis. J Exp Bot 2010; 61: 2469–78.Web of ScienceCrossrefGoogle Scholar

  • 28.

    Holk A, Rietz S, Zahn M, Quader H, Scherer GFE. Molecular identification of cytosolic, patatin-related phospholipases A from Arabidopsis with potential functions in plant signal transduction. Plant Physiol 2002; 130: 90–101.PubMedCrossrefGoogle Scholar

  • 29.

    Li M, Bahn SC, Fan C, Li J, Phan T, Ortiz M, Roth M, Welti R, Jaworski J, Wang X. Patatin-related phospholipase pPLA-IIIδ increases seed oil content with long chain fatty acids in Arabidopsis. Plant Physiol 2013; 162: 39–51.Google Scholar

  • 30.

    Yang WY, Zheng Y, Bahn SC, Pan XQ, Li MY, Vu HS, Roth MR, Scheu B, Welti R, Hong YY, Wang XM. The patatin-containing phospholipase A pPLA-IIα modulates oxylipin formation and water loss in Arabidopsis thaliana. Mol Plant 2012; 5: 452–60.CrossrefGoogle Scholar

  • 31.

    Li MY, Bahn SC, Guo L, Musgrave W, Berg H, Welti R, Wang XM. Patatin-related phospholipase pPLA-IIIβ-induced changes in lipid metabolism alter cellulose content and cell elongation in Arabidopsis. Plant Cell 2011; 23: 1107–23.CrossrefGoogle Scholar

  • 32.

    La Camera S, Geoffroy P, Samaha H, Ndiaye A, Rahim G, Legrand M, Heitz T. A pathogen-inducible patatin-like lipid acyl hydrolase facilitates fungal and bacterial host colonization in Arabidopsis. Plant J 2005; 44: 810–25.Google Scholar

  • 33.

    Noiriel A, Benveniste P, Banas A, Stymne S, Bouvier-Nave P. Expression in yeast of a novel phospholipase A1 cDNA from Arabidopsis thaliana. Eur J Biochem 2004; 3752–64.PubMedGoogle Scholar

  • 34.

    Shayman JA, Kelly R, Kollmeyer J, He Y, Abe A. Group XV phospholipase A2, a lysosomal phospholipase A2. Prog Lipid Res 2011; 50: 1–13.Web of SciencePubMedCrossrefGoogle Scholar

  • 35.

    Mansfeld J, Ulbrich-Hofmann R. Secretory phospholipase A2-α from Arabidopsis thaliana: functional parameters and substrate preference. Chem Phys Lipids 2007; 150: 156–66.Web of ScienceGoogle Scholar

  • 36.

    Mariani ME, Villarreal MA, Cheung F, Leiva EPM, Madoery RR, Fidelio GD. In silico and in vitro characterization of phospholipase A2 isoforms from soybean (Glycine max). Biochimie 2012; 94: 2608–19.PubMedCrossrefWeb of ScienceGoogle Scholar

  • 37.

    Fujikawa Y, Fujikawa R, Iijima N, Esaka M. Characterization of secretory phospholipase A2 with phospholipase A1 activity in tobacco, Nicotiana tabacum (L.). Lipids 2012; 47: 303–12.Web of SciencePubMedCrossrefGoogle Scholar

  • 38.

    Verlotta A, Liberatore MT, Cattivelli L, Trono D. Secretory phospholipases A2 in durum wheat (Triticum durum Desf.): gene expression, enzymatic activity, and relation to drought stress adaptation. Int J Mol Sci 2013; 14: 5146–69.CrossrefWeb of ScienceGoogle Scholar

  • 39.

    Yang W, Devaiah SP, Pan X, Isaac G, Welti R, Wang X. AtPLAI is an acyl hydrolase involved in basal jasmonic acid production and Arabidopsis resistance to Botrytis cinerea. J Biol Chem 2007; 282: 18116–28.Web of ScienceGoogle Scholar

  • 40.

    Rietz S, Dermendjiev G, Oppermann E, Tafesse FG, Effendi Y, Holk A, Parker JE, Teige M, Scherer GF. Roles of Arabidopsis patatin-related phospholipases A in root development are related to auxin responses and phosphate deficiency. Mol Plant 2010; 3: 524–38.PubMedCrossrefGoogle Scholar

  • 41.

    Scherer GFE. Phospholipase A in plant signal transduction. Lipid Signal Plants 2010; 6: 3–22.Google Scholar

  • 42.

    Dennis EA, Cao J, Hsu YH, Magrioti V, Kokotos G. Phospholipase A2 enzymes: physical structure, biological function, disease implication, chemical inhibition, and therapeutic intervention. Chem Rev 2011; 111: 6130–85.CrossrefWeb of SciencePubMedGoogle Scholar

  • 43.

    Hong YW, Wang TW, Hudak KA, Schade F, Froese CD, Thompson JE. An ethylene-induced cDNA encoding a lipase expressed at the onset of senescence. Proc Natl Acad Sci USA 2000; 97: 8717–22.CrossrefGoogle Scholar

  • 44.

    Kato T, Morita MT, Fukaki H, Yamauchi Y, Uehara M, Niihama M, Tasaka M. SGR2, a phospholipase-like protein, and ZIG/SGR4, a SNARE, are involved in the shoot gravitropism of Arabidopsis. Plant Cell 2002; 14: 33–46.CrossrefGoogle Scholar

  • 45.

    Scherer GFE. Secondary messengers and phospholipase A2 in auxin signal transduction. Plant Mol Biol 2002; 49: 357–72.PubMedCrossrefGoogle Scholar

  • 46.

    Ackermann EJ, Kempner ES, Dennis EA. Ca2+-independent cytosolic phospholipase A2 from macrophage-like P388D1 cells – isolation and characterization. J Biol Chem 1994; 269: 9227–33.Google Scholar

  • 47.

    La Camera S, Balague C, Gobel C, Geoffroy P, Legrand M, Feussner I, Roby D, Heitz T. The Arabidopsis patatin-like protein 2 (PLP2) plays an essential role in cell death execution and differentially affects biosynthesis of oxylipins and resistance to pathogens. Mol Plant Microbe Interact 2009; 22: 469–81.Web of ScienceGoogle Scholar

  • 48.

    Cacas JL, Vailleau F, Davoine C, Ennar N, Agnel JP, Tronchet M, Ponchet M, Blein JP, Roby D, Triantaphylides C, Montillet JL. The combined action of 9 lipoxygenase and galactolipase is sufficient to bring about programmed cell death during tobacco hypersensitive response. Plant Cell and Environ 2005; 28: 1367–78.Google Scholar

  • 49.

    Ellinger D, Kubigsteltig II. Involvement of DAD1-like lipases in response to salt and osmotic stress in Arabidopsis thaliana. Plant Signal Behav 2010; 5: 1269–71.CrossrefGoogle Scholar

About the article

Corresponding author: Randall J. Weselake, Alberta Innovates Phytola Centre, Department of Agricultural, Food and Nutritional Science, 410 Agriculture/Forestry Centre, University of Alberta, Edmonton, Alberta, Canada T6G 2P5, e-mail:

Received: 2013-05-07

Accepted: 2013-06-25

Published Online: 2013-07-23

Published in Print: 2013-10-01

Citation Information: BioMolecular Concepts, Volume 4, Issue 5, Pages 527–532, ISSN (Online) 1868-503X, ISSN (Print) 1868-5021, DOI: https://doi.org/10.1515/bmc-2013-0011.

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