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Information on EC 3.1.4.4 - phospholipase D and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LRZ5
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3.1.4.4 phospholipase DIUBMB Comments
Also acts on other phosphatidyl esters.
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Word Map
- 3.1.4.4
-
phosphatidic
- diacylglycerol
- pkc
-
liposomal
- doxorubicin
- agonist
-
pegylated
-
phorbol
- phospholipases
-
transphosphatidylation
- 12-myristate
-
adp-ribosylation
- 13-acetate
- pertussis
-
phosphohydrolase
-
arachidonic
- propranolol
- phosphoinositide
-
gtp-binding
- fmlp
-
prelabeled
- anandamide
- rhoa
- 1-butanol
-
endocannabinoids
- staurosporine
-
lysophosphatidic
- pc-plc
-
phosphatidylcholine-specific
-
latissimus
- diglyceride
- pkcalpha
-
phosphatidylinositol-specific
- pseudotuberculosis
- 1,2-diacylglycerol
- arf6
- cannabinoids
-
fmet-leu-phe
-
listening
-
fmlp-stimulated
-
platinum-resistant
- analysis
-
phosphoinositide-specific
- gtpgammas
- synthesis
-
3hcholine
-
hand-foot
-
platinum-sensitive
-
fmlp-induced
- lymphadenitis
- medicine
-
ptdins4,5p2
- molecular biology
- 5-kinase
- agriculture
- biotechnology
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
pld, phospholipase d, nape-pld, phospholipase d1, dermonecrotic toxin, phospholipase d2, pc-pld, pldalpha, rpld1, spo14, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AtPLDalpha1
AtPLDalpha2
-
-
-
-
AtPLDbeta1
-
-
-
-
AtPLDbeta2
-
-
-
-
AtPLDdelta
AtPLDepsilon
-
-
-
-
AtPLDgamma1
-
-
-
-
AtPLDgamma2
-
-
-
-
AtPLDgamma3
-
-
-
-
AtPLDp1
-
-
-
-
AtPLDp2
-
-
-
-
AtPLDzeta
-
-
-
-
choline phosphatase
-
-
-
-
hPLD1
-
-
-
-
hPLD2
-
-
-
-
lecithinase D
-
-
-
-
lipophosphodiesterase II
-
-
-
-
Meiosis-specific sporulation protein SPO14
-
-
-
-
mPLD1
-
-
-
-
mPLD2
-
-
-
-
Phosphatidylcholine-hydrolyzing phospholipase D1
-
-
-
-
Phosphatidylcholine-hydrolyzing phospholipase D2
-
-
-
-
Phospholipase D1 PHOX and PX containing domain
-
-
-
-
Phospholipase D2 PHOX and PX containing domain
-
-
-
-
phospholipase Dalpha1
phospholipase Dalpha3
PLD
PLD delta
-
-
-
-
PLD epsilon
-
-
-
-
PLD zeta
-
-
-
-
PLD1C
-
-
-
-
PLDalpha
PLDalpha1
PLDalpha3
PLDbeta
PLDdelta1
-
-
-
-
PLDzeta1
-
-
-
-
PLDzeta2
rPLD1
-
-
-
-
rPLD2
-
-
-
-
AtPLDalpha1
-
-
-
-
AtPLDdelta
-
-
-
-
PLD
-
-
-
-
PLDalpha
-
-
-
-
PLDalpha3
-
-
-
-
PLDbeta
-
-
-
-
PLDzeta2
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
phosphatidylcholine phosphatidohydrolase
Also acts on other phosphatidyl esters.
CAS REGISTRY NUMBER
COMMENTARY
9001-87-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidate + choline
-
-
-
?
glycosylinositol phosphoceramide + H2O
phytoceramide-1-phosphate + glycosylinositol
-
-
phytoceramide-1-phosphate with an alpha-hydroxy fatty acid
-
?
phosphatidylethanolamine + H2O
ethanolamine + phosphatidic acid
-
-
-
-
?
phosphatidylglycerol + H2O
phosphatidate + glycerol
enzyme shows the highest activity toward phosphatidylcholine and the lowest toward phosphatidylserine
-
-
?
phosphatidylserine + H2O
phosphatidate + serine
enzyme shows the highest activity toward phosphatidylcholine and the lowest toward phosphatidylserine
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
presence of phosphatidylinositol 4,5-bisphosphate and phosphatidylethanol is required
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
phosphatidic acid binds to ABI1, a PP2C, which functions as a negative regulator in abscisic acid signalling in stomata closure. Phosphatidic acid stimulated NADPH oxidase activity and reactive oxygen species production in wild-type and PLDalpha1-deficient cells, cellular and physiological effects of phosphatidic acid, overview
-
?
phosphatidylcholine + H2O
phosphatidate + choline
enzyme shows the highest activity toward phosphatidylcholine and the lowest toward phosphatidylserine
-
-
?
additional information
?
-
-
phospholipid acyl composition in wild type and enzyme-suppressed mutants
-
?
additional information
?
-
-
involved in wound-induced metabolism of polyunsaturated fatty acids
-
?
additional information
?
-
-
hydrolysis of phosphatidylcholine by enzyme isoforms PLDzeta1 and PLDzeta2 during phosphorus starvation contributes to the supply of inorganic phosphorus for cell metabolism and diacylglycerol moieties for galactolipid synthesis
-
-
?
additional information
?
-
-
incubation of Arabidopsis thaliana cell suspensions with primary alcohols inhibit the induction of two salicylic acid-responsive genes, PR1 and WRKY38, in a dose dependent manner. This inhibitory effect is more pronounced when the primary alcohols are more hydrophobic. Secondary or tertiary alcohols have no inhibitory effect. These results show that PLD activity is upstream of the induction of these genes by salicylic acid. A detailed analysis of the regulation of salicylic acid-responsive genes show that PLD can act both positively and negatively, either on gene induction or gene repression
-
-
?
additional information
?
-
-
PLDalpha1 interacts with the Galpha1 subunit of the heterotrimeric G protein to inhibit stomatal opening
-
-
?
additional information
?
-
-
the different PLDs exhibit distinguishable reaction conditions, substrate preferences and subcellular localization, overview. PLDalpha1 interacts with Galpha protein, a heterotrimeric Galpha protein to prevent closed stomata from opening
-
-
?
additional information
?
-
-
in presence of primary alcohols, such as 1-butanol or ethanol, PLD also has a unique ability to transfer phosphatidyl group to a primary alcohol to form phosphatidylalcohol at the expense of phosphatidic acid
-
-
?
additional information
?
-
-
isozyme PLDalpha3 hydrolyzes multiple substrates with distinguishable preferences
-
-
?
additional information
?
-
-
PLDepsilon is active under a broad range of reaction conditions
-
-
?
additional information
?
-
-
the enzyme hydrolyzes glycosylinositol phosphoceramide specifically, but not glycerophospholipids, phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, or sphingomyelin, MALDI-TOF mass spectrometry product identification, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphatidylethanolamine + H2O
ethanolamine + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
-
phosphatidic acid binds to ABI1, a PP2C, which functions as a negative regulator in abscisic acid signalling in stomata closure. Phosphatidic acid stimulated NADPH oxidase activity and reactive oxygen species production in wild-type and PLDalpha1-deficient cells, cellular and physiological effects of phosphatidic acid, overview
-
?
additional information
?
-
-
involved in wound-induced metabolism of polyunsaturated fatty acids
-
?
additional information
?
-
-
hydrolysis of phosphatidylcholine by enzyme isoforms PLDzeta1 and PLDzeta2 during phosphorus starvation contributes to the supply of inorganic phosphorus for cell metabolism and diacylglycerol moieties for galactolipid synthesis
-
-
?
additional information
?
-
-
incubation of Arabidopsis thaliana cell suspensions with primary alcohols inhibit the induction of two salicylic acid-responsive genes, PR1 and WRKY38, in a dose dependent manner. This inhibitory effect is more pronounced when the primary alcohols are more hydrophobic. Secondary or tertiary alcohols have no inhibitory effect. These results show that PLD activity is upstream of the induction of these genes by salicylic acid. A detailed analysis of the regulation of salicylic acid-responsive genes show that PLD can act both positively and negatively, either on gene induction or gene repression
-
-
?
additional information
?
-
-
PLDalpha1 interacts with the Galpha1 subunit of the heterotrimeric G protein to inhibit stomatal opening
-
-
?
additional information
?
-
-
the different PLDs exhibit distinguishable reaction conditions, substrate preferences and subcellular localization, overview. PLDalpha1 interacts with Galpha protein, a heterotrimeric Galpha protein to prevent closed stomata from opening
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
additional information
no requirement for Ca2+ or other divalent cation
Ca2+
-
interacts with the catalytic regions of the enzyme. PLDbetacat (PLD with a deleted regulatory C2 domain) exhibits Ca2+-dependent activity, is much less active and requires a higher level of Ca2+ than the full-length enzyme PLDbeta. The interaction of Ca2+ with PLDbetacat (PLD with a deleted regulatory C2 domain) increases the affinity of the protein for the activator phosphatidylinositol 4,5-bisphosphate. Ca2+ binding to the C2 domain stimulates phosphatidylcholine binding but inhibits phosphatidylinositol 4,5-bisphosphate
Ca2+
required, highest activity in presence of micromolar concentrations
Ca2+
the C2 domain binds phosphatidylglycerol in a Ca2+-independent manner while phosphatidic acid and phosphatidylserine binding are enhanced in the presence of Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-butanol
-
mediates differential effects on cellular organization and seedling growth, in part through the differential modulation of specific isoforms of phospholipase D. 1-Butanol induces more pronounced modifications in cytoskeletal organization, seedling growth, and cell division at concentrations severalfold higher than N-lauroylethanolamine
ethanol
-
suppression of PLD-mediated phosphatidic acid formation by alcohol alleviated the growth-promoting effect of PLDepsilon
N-lauroylethanolamine
-
mediates differential effects on cellular organization and seedling growth, in part through the differential modulation of specific isoforms of phospholipase D. 1-Butanol induces more pronounced modifications in cytoskeletal organization, seedling growth, and cell division at concentrations severalfold higher than N-lauroylethanolamine
Triton X-100
complete loss of activity and prohibition of any stimulation by phosphatidylinositol 4,5-bisphosphate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
oleic acid
best stimulation, optimal at 0.5 mM, stimulates binding to substrate, in presence of Ca2+
phosphatidylinositol-4,5-bisphosphate
less than oleic acid, best at 0.03 mM
phosphoinositide-4,5-bisphosphate
-
i.e. PIP2, phosphoinositides, particularly PIP2, another key regulator of PLD activation are required by PLDbeta, PLDgamma, PLDdelta, and PLDzeta for activity
salicylic acid
-
activates transphosphatidylation reaction of PLD in a dose-dependent manner
phosphatidylinositol 4,5-bisphosphate
-
the interaction of Ca2+ with PLDbetacat (PLD with a deleted regulatory C2 domain) increases the affinity of the protein for the activator phosphatidylinositol 4,5-bisphosphate. Ca2+ binding to the C2 domain stimulates phosphatidylcholine binding but inhibits phosphatidylinositol 4,5-bisphosphate
phosphatidylinositol 4,5-bisphosphate
-
PLDbeta, PLDgamma, PLDdelta, and PLDzeta require PIP2 for activity
additional information
no requirement for phosphatidylethanolamine in substrate vesicles, comparison of isozymes
-
additional information
no activation by stearic or palmitic acid
-
additional information
-
activity of phospholipase D in plants increases under different hyperosmotic stresses, such as dehydration, drought, and salinity, overview
-
additional information
-
PLDepsilon activity and phosphatidic acid content enhance growth under hyperosmotic stres
-
additional information
-
cold stress treatment strongly stimulates the phospholipase D activity and affects the phosphatidic acid levels of the plasma membranes. Concommitantly, the H+-ATPase activity is strongly inhibited, which correlates with a reduced association with the regulatory 14-3-3 proteins
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
5-day-old cell suspensions cultures of Arabidopsis thaliana, ecotype Columbia-0 are used
-
isozyme PLDalpha1 is presented in guard cells in a much higher level than other PLDs in Arabidopsis thaliana
root of growing seedling, accumulation of enzyme in the root cap and the rhizodermis. Expression in the rhizodermis is considerably higher in trichoblasts before and during root hair formation and growth
-
quantitative profiling of molecular species of polar glycerolipids. In response to phosphorus starvation, concentration of phospholipids is decreased and that of galactolipids is increased
expression is 1000fold higher than that of isoenzyme PLDalpha3
expression is 1000fold lower than that of isoenzyme PLDalpha1
expression is 1000fold higher than that of isoenzyme PLDalpha3
expression is 1000fold lower than that of isoenzyme PLDalpha1
both AtPLDalpha 1 and AtPLDdelta are found to be activated in response to salt stress
expression is 1000fold higher than that of isoenzyme PLDalpha3
expression is 1000fold lower than that of isoenzyme PLDalpha1
-
quantitative profiling of molecular species of polar glycerolipids. In response to phosphorus starvation, concentration of phospholipids is decreased and that of galactolipids is increased
expression is 1000fold higher than that of isoenzyme PLDalpha3
expression is 1000fold lower than that of isoenzyme PLDalpha1
-
localization of isozyme pLDzeta2 in epidermal cells in the distal root elongation zone and lateral root cap cells adjacent to them
root of growing seedling, accumulation of enzyme in the root cap and the rhizodermis
expression is 1000fold higher than that of isoenzyme PLDalpha3
expression is 1000fold lower than that of isoenzyme PLDalpha1
expression is 1000fold higher than that of isoenzyme PLDalpha3
expression is 1000fold lower than that of isoenzyme PLDalpha1
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
cytoplasmic localization in root cap cells and in cells of the root transition zone as well as in aerial parts of the plant. PLD is associated with both microtubules and clathrin-coated vesicles and pits
in dividing cells of root apical meristem and leaf petiole epidermis, enzyme is enriched in mitotic spindles and phragmoplasts
in dividing cells of root apical meristem and leaf petiole epidermis, enzyme is enriched in mitotic spindles and phragmoplasts
N-terminal regulatory domain of protein is sufficient for sorting to the tonoplast. Under phosphate deprivation, PLDzeta2 remains localized to the tonoplast, but its distribution is uneven and preferentially close to mitochondria and beside chloroplasts
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the sites of phospholipid hydrolysis by phospholiphosphatidic acids D, C, A, and the targets of phosphatidic acid identified in plants that are potentially involved in hyperosmotic stress responses, and regulation of PLD isozymes in hyperosmotic stresses, overview
physiological function
physiological function
-
involvement of isozyme phospholipase Dzeta2 in root hydrotropism through the suppression of root gravitropism by abscisic acid, overview
physiological function
-
involvement of PLD in response to water deficits and salinity. Isozyme PLDdelta plays an important role in protecting cells from damage by reactive oxygen species. Isozyme PLDalpha1 promotes stomatal closure and reduces water loss. PLDalpha1 and PLDdelta are involved in seedling tolerance to salt stress. PLDalpha3 and PLDepsilon enhance plant growth and hyperosmotic tolerance. The different PLDs regulate the production of phosphatidic acid, a key class of lipid mediators in plant response to environmental stresses. Signalling and regulatory functions of PLD isozymes and phosphatidic acid in Arabidopsis thaliana response to drought and salinity, overview. PLDalpha1 and phosphatidic acid play a positive role in abscisic acid effects on preventing water loss. Involvement of PLDalpha3 in salt stress response, and of isozyme PLDepsilon in N signalling and plant growth under salt stress and water deficiency with genetic alterations of PLDepsilon affecting plant root architecture and biomass production, overview
physiological function
-
isozyme PLDalpha3 plays a positive role in hyperosmotic stress through a mechanism different from that for PLDalpha1, which mediates the effect of abscisic acid on stomatal movements. PLDalpha3 enhances root growth and accelerates flowering time under hyperosmotic stress. Alterations of PLDalpha3 activity affect the level of phosphatidic acid, and of transcripts of TOR and AGC2.1, of ABA-responsive genes, and of phosphorylated S6K protein under hyperosmotic stress, overview. PLDalpha3 may be involved in the crosstalk among glucose sensing, abscisic acid response, and S6K activation to regulate growth and development
physiological function
-
PLDepsilon and phosphatidic acid promote organism growth and play a role in nitrogen signaling. The lipid-signaling process may play a role in connecting membrane sensing of nutrient status to increased plant growth and biomass production
physiological function
-
role of PLDalpha1 in promoting abscisic acid sensitivity and stomatal closure. PLDalpha1 and phosphatidic acid regulate stomatal closure via a bifurcating pathway and interacts with the Galpha1 subunit of the heterotrimeric G protein to inhibit stomatal opening. PLDalpha1-derived phosphatidic acid binds to ABI1, a protein phosphatase 2C, that functions as a negative regulator in the abscisic acid signaling pathway, overview
physiological function
-
PLDalpha1 promotes stomatal closure and reduces water loss. PLDalpha1 and PLDdelta are involved in seedling tolerance to salt stress. PLDalpha3 and PLDepsilon enhance plant growth and hyperosmotic tolerance. The different PLDs regulate the production of phosphatidic acid that is a key class of lipid mediators in plant response to environmental stresses. PLD-produced phosphatidic acids and its molecular targets in hyperosmotic stress responses, overview. PLDdelta plays a role in plant response to reactive oxygen species, dehydration, and salt stresses, while PLDepsilon plays a role in N signalling and plant growth under salt stress and water deficiency, and PLDalpha3 in salt and mild drought responses
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PLDZ1_ARATH
1096
0
124505
Swiss-Prot
Chloroplast (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
comparison of domain structures of isozymes
?
x * 90000, SDS-PAGE, x * 88100, calculated from sequence. X * 14800, isolated C2 domain, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
sequence contains one potential N-glycosylation site
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA1-158
-
PLD with a deleted regulatory C2 domain exhibits Ca2+-dependent activity, is much less active and requires a higher level of Ca2+ than the full-length enzyme PLDbeta
R611D
loss of more than 80% of phosphatidylinositol-stimulated activity, 50% of oleate-stimulated activity
additional information
additional information
-
construction of GST fusion proteins containing parts of the enzyme, identification of a phosphatidylinositol-binding region, deletion of this region abolishes enzyme activity
additional information
-
enzyme suppressed ecotype, mechanical wounding of leaves results in significantly less hydrolysis of phosphatidylcholine than in wild type, phospholipid acyl composition in wild type and enzyme-suppressed mutants
additional information
-
expression and characterization of putative C2 domains and structural features
additional information
-
disruption of isoforms PLDzeta2 and PLDzeta1 function results in a smaller decrease in phosphatidylcholine and a smaller increase in digalactosyldiacylglycerol in phosphorus-starved roots
additional information
enzyme-deficient mutant shows proliferation of membranes inside the vacuole
additional information
-
enzyme-deficient mutant shows proliferation of membranes inside the vacuole
additional information
Atpldalpha 1 and AtPLDdelta single and double knock-out mutants exhibit enhanced sensitivity to high salinity stress in a plate assay. Both PLDs are activated upon dehydration and the knock-out mutants are hypersensitive to hyperosmotic stress, displaying strongly reduced growth
additional information
Atpldalpha 1 and AtPLDdelta single and double knock-out mutants exhibit enhanced sensitivity to high salinity stress in a plate assay. Both PLDs are activated upon dehydration and the knock-out mutants are hypersensitive to hyperosmotic stress, displaying strongly reduced growth
additional information
knockout and overexpression of PLDalpha3 alter plant response to salinity and water deficit. Alterations of PLDalpha3 result in changes in phosphatidic acid level and membrane lipid composition. PLDalpha3-knockout plants display increased sensitivities to salinity and water deficiency and also tend to induce abscisic acid-responsive genes more readily than wild-type plants, whereas PLDalpha3-overexpressed plants have decreased sensitivities. PLDalpha3-knockout plants flower later than wild-type plants in slightly dry conditions, whereas PLDalpha3-overexpressed plants flower earlier
additional information
knockout and overexpression of PLDalpha3 alter plant response to salinity and water deficit. Alterations of PLDalpha3 result in changes in phosphatidic acid level and membrane lipid composition. PLDalpha3-knockout plants display increased sensitivities to salinity and water deficiency and also tend to induce abscisic acid-responsive genes more readily than wild-type plants, whereas PLDalpha3-overexpressed plants have decreased sensitivities. PLDalpha3-knockout plants flower later than wild-type plants in slightly dry conditions, whereas PLDalpha3-overexpressed plants flower earlier
additional information
-
knockout and overexpression of PLDalpha3 alter plant response to salinity and water deficit. Alterations of PLDalpha3 result in changes in phosphatidic acid level and membrane lipid composition. PLDalpha3-knockout plants display increased sensitivities to salinity and water deficiency and also tend to induce abscisic acid-responsive genes more readily than wild-type plants, whereas PLDalpha3-overexpressed plants have decreased sensitivities. PLDalpha3-knockout plants flower later than wild-type plants in slightly dry conditions, whereas PLDalpha3-overexpressed plants flower earlier
additional information
PLD activity during the wounding response is restricted to the ruptured cells using 32P-labelled phospholipid analyses of Arabidopsis pld knock-out mutants and PLD-silenced tomato cell-suspension cultures. plda1 knock-out lines have reduced wounding-induced phosphatidic acid production, and the remainder is completely eliminated in a plda1/d double knock-out line
additional information
-
gene pldzeta2 mutations significantly retard or disturb root hydrotropic responses, but cause no morphological abnormality, inhibitory effect of abscisic acid on gravitropism is affected in pldf2 mutant roots. Construction of transgenic Arabidopsis thaliana plants expressing the isozyme via transfection by Agrobacterium tumefaciens LBA4404
additional information
-
isozyme PLDdelta-KO cells exhibit a higher rate of H2O2-induced cell death than the wild-type. Unlike PLDalpha1-KO plants, PLDdelta-KO plants are still able to produce the normal levels of reactive oxygen species in response to stresses, such as abscisic acid and freezing. The stomata in epidermal peels from PLDalpha1-deficient Arabidopsis thaliana plants fail to close in response to abscisic acid, whereas external supply of phosphatidic acid, the lipid product of PLD, promotes the stomatal closure in wild-type and PLDalpha1-deficient Arabidopsis thaliana plants. PLDalpha3-KO plants accumulate a similar level of abscisic acid as the wild-type, but display higher levels of abscisic acid response gene expression. The root growth of PLDalpha3-KO seedlings is also more inhibited by abscisic acid treatment than wild-type
additional information
-
knockout of PLDepsilon decreases root growth and biomass accumulation, whereas overexpression of PLDepsilon enhances root growth and biomass accumulation. Increased expression of PLDepsilon also promotes root hair elongation and primary root growth under severe nitrogen deprivation. Growth phenotypes of PLDepsilon mutant seedlings under different conditions, detailed overview
additional information
-
Nicotiana tabacum transgenic plants, overexpressing Arabidopsis thaliana isozyme PLDalpha1, display more susceptibility to drought than control plants, drought also induces an increase in PLDa1 activity. High level of PLDalpha1 activity is correlated to membrane degradation in late stages of drought, as demonstrated by ionic leakage and lipid peroxidation. Recombinant PLD2 promotes stomatal closure at earlier stages, but disrupts membranes in prolonged drought stress, phenotype, overview
additional information
-
PLDalpha3-knockout plants are less tolerant to salt stress than wild-type plants. In addition, under water deficit conditions, PLDalpha3-KO plants flower later, whereas PLDalpha3-overexpressing plants flower earlier than wild-type plants. PLDalpha3-KO seeds and seedlings are less sensitive to glucose, whereas overexpression of PLDalpha3 enhances glucose sensitivity compared to the wild-type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified from plant proteins by immunoaffinity column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Arabidopsis thaliana as a His-tagged fusion protein
expression of mature-like form of the C2 domain in Escherichia coli
expression of protein in Pichia pastoris, expression of mature-like form of the C2 domain in Escherichia coli
functional overexpression of isozyme PLDalpha1 in Nicotiana tabacum transgenic plants under the control of the 35S promoter
-
gene pldzeta2, expression of isozyme pLDzeta2 in Escherichia coli. Construction of transgenic Arabidopsis thaliana plants expressing the isozyme via transfection by Agrobacterium tumefaciens LBA4404
-
wild-type PLDbeta, PLDbetacat with a deleted C2 domain, expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
knockout and overexpression of PLDalpha3 alter plant response to salinity and water deficit. Alterations of PLDalpha3 result in changes in phosphatidic acid level and membrane lipid composition. PLDalpha3-knockout plants display increased sensitivities to salinity and water deficiency and also tend to induce abscisic acid-responsive genes more readily than wild-type plants, whereas PLDalpha3-overexpressed plants have decreased sensitivities. PLDalpha3-knockout plants flower later than wild-type plants in slightly dry conditions, whereas PLDalpha3-overexpressed plants flower earlier
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zheng, L.; Shan, J.; Krishnamoorthi, R.; Wang, X.
Activation of plant phospholipase Dbeta by phosphatidylinositol 4,5-bisphosphate: Characterization of binding site and mode of action
Biochemistry
41
4546-4553
2002
Arabidopsis thaliana
Zien, C.A.; Wang, C.; Wang, X.; Welti, R.
In vivo substrates and the contribution of the common phospholipase D, PLDa, to wound-induced metabolism of lipids in Arabidopsis
Biochim. Biophys. Acta
1530
236-248
2001
Arabidopsis thaliana
Zheng, L.; Krishnamoorthi, R.; Zolkiewski, M.; Wang, X.
Distinct Ca2+ binding properties of novel C2 domains of plant phospholipase D.alpha. and b
J. Biol. Chem.
275
19700-19706
2000
Arabidopsis thaliana
Wang, C.; Wang, X.
A novel phospholipase D of Arabidopsis that is activated by oleic acid and associated with the plasma membrane
Plant Physiol.
127
1102-1112
2001
Arabidopsis thaliana (Q9C5Y0)
Qin, C.; Wang, X.
The Arabidopsis phospholipase D family. Characterization of a calcium-independent and phosphatidylcholine-selective PLD zeta 1 with distinct regulatory domains
Plant Physiol.
128
1057-1068
2002
Arabidopsis thaliana (Q9LRZ5)
Pappan, K.; Zheng, L.; Krishnamoorthi, R.; Wang, X.
Evidence for and characterization of Ca2+ binding to the catalytic region of Arabidopsis thaliana phospholipase Dbeta
J. Biol. Chem.
279
47833-47839
2004
Arabidopsis thaliana
Motes, C.M.; Pechter, P.; Yoo, C.M.; Wang, Y.S.; Chapman, K.D.; Blancaflor, E.B.
Differential effects of two phospholipase D inhibitors, 1-butanol and N-acylethanolamine, on in vivo cytoskeletal organization and Arabidopsis seedling growth
Protoplasma
226
109-123
2005
Arabidopsis thaliana
Qin, C.; Li, M.; Qin, W.; Bahn, S.C.; Wang, C.; Wang, X.
Expression and characterization of Arabidopsis phospholipase Dgamma 2
Biochim. Biophys. Acta
1761
1450-1458
2006
Arabidopsis thaliana (Q9T051), Arabidopsis thaliana (Q9T053), Arabidopsis thaliana
Yamaryo, Y.; Dubots, E.; Albrieux, C.; Baldan, B.; Block, M.A.
Phosphate availability affects the tonoplast localization of PLDzeta2, an Arabidopsis thaliana phospholipase D
FEBS Lett.
582
685-690
2008
Arabidopsis thaliana (Q9M9W8), Arabidopsis thaliana
Li, M.; Welti, R.; Wang, X.
Quantitative profiling of Arabidopsis polar glycerolipids in response to phosphorus starvation. Roles of phospholipases D zeta1 and D zeta2 in phosphatidylcholine hydrolysis and digalactosyldiacylglycerol accumulation in phosphorus-starved plants
Plant Physiol.
142
750-761
2006
Arabidopsis thaliana
Hong, Y.; Pan, X.; Welti, R.; Wang, X.
Phospholipase Dalpha3 is involved in the hyperosmotic response in Arabidopsis
Plant Cell
20
803-816
2008
Arabidopsis thaliana (Q38882), Arabidopsis thaliana (Q9C888), Arabidopsis thaliana
Bargmann, B.O.; Laxalt, A.M.; Riet, B.; Testerink, C.; Merquiol, E.; Mosblech, A.; Reyes, A.L.; Pieterse, C.M.; Haring, M.A.; Heilmann, I.; Bartels, D.; Munnik, T.
Reassessing the role of phospholipase D in the Arabidopsis wounding response
Plant Cell Environ.
32
837-850
2009
Arabidopsis thaliana (Q38882)
Bargmann, B.O.; Laxalt, A.M.; ter Riet, B.; van Schooten, B.; Merquiol, E.; Testerink, C.; Haring, M.A.; Bartels, D.; Munnik, T.
Multiple PLDs required for high salinity and water deficit tolerance in plants
Plant Cell Physiol.
50
78-89
2009
Solanum lycopersicum, Arabidopsis thaliana (Q38882), Arabidopsis thaliana (Q9C5Y0)
Krinke, O.; Flemr, M.; Vergnolle, C.; Collin, S.; Renou, J.P.; Taconnat, L.; Yu, A.; Burketova, L.; Valentova, O.; Zachowski, A.; Ruelland, E.
Phospholipase D activation is an early component of the salicylic acid signaling pathway in Arabidopsis thaliana cell suspensions
Plant Physiol.
150
424-436
2009
Arabidopsis thaliana
Hong, Y.; Zheng, S.; Wang, X.
Dual functions of phospholipase Dalpha1 in plant response to drought
Mol. Plant
1
262-269
2008
Arabidopsis thaliana
Hong, Y.; Zhang, W.; Wang, X.
Phospholipase D and phosphatidic acid signalling in plant response to drought and salinity
Plant Cell Environ.
33
627-635
2009
Arabidopsis thaliana
Hong, Y.; Devaiah, S.P.; Bahn, S.C.; Thamasandra, B.N.; Li, M.; Welti, R.; Wang, X.
Phospholipase D epsilon and phosphatidic acid enhance Arabidopsis nitrogen signaling and growth
Plant J.
58
376-387
2009
Arabidopsis thaliana
Hong, Y.; Pan, X.; Welti, R.; Wang, X.
The effect of phospholipase Dalpha3 on Arabidopsis response to hyperosmotic stress and glucose
Plant Signal. Behav.
3
1099-1100
2008
Arabidopsis thaliana
Taniguchi, Y.Y.; Taniguchi, M.; Tsuge, T.; Oka, A.; Aoyama, T.
Involvement of Arabidopsis thaliana phospholipase Dzeta2 in root hydrotropism through the suppression of root gravitropism
Planta
231
491-497
2010
Arabidopsis thaliana
Tanaka, T.; Kida, T.; Imai, H.; Morishige, J.; Yamashita, R.; Matsuoka, H.; Uozumi, S.; Satouchi, K.; Nagano, M.; Tokumura, A.
Identification of a sphingolipid-specific phospholipase D activity associated with the generation of phytoceramide-1-phosphate in cabbage leaves
FEBS J.
280
3797-3809
2013
Arabidopsis thaliana, Brassica oleracea, Capsella bursa-pastoris
Rahier, R.; Noiriel, A.; Abousalham, A.
Functional characterization of the N-terminal C2 domain from Arabidopsis thaliana phospholipase Dalpha and Dbeta
BioMed Res. Int.
2016
2721719
2016
Arabidopsis thaliana (P93733), Arabidopsis thaliana (Q38882)
Novak, D.; Vadovic, P.; Ovecka, M.; Samajova, O.; Komis, G.; Colcombet, J.; Samaj, J.
Gene expression pattern and protein localization of Arabidopsis phospholipase D alpha 1 revealed by advanced light-sheet and super-resolution microscopy
Front. Plant Sci.
9
371
2018
Arabidopsis thaliana (Q38882), Arabidopsis thaliana
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