Pld is the Drosophila phospholipase D that hydrolyzes phosphatidylcholine to generate phosphatidic acid. This lipid-signaling enzyme supports Golgi organization, secretory-vesicle trafficking and membrane delivery during cellularization, and contributes to phosphoinositide homeostasis and photoreceptor function. It localizes to the cytoplasm and small cytoplasmic vesicles in cellularizing embryos.
Summary: The experimentally characterized reaction is D-type glycerophospholipid hydrolysis. Replace generic catalytic activity with the specific existing enzyme term.
Reason: The experimentally characterized reaction is D-type glycerophospholipid hydrolysis. Replace generic catalytic activity with the specific existing enzyme term.
D. melanogaster Pld exhibits classic Pld activity, increases its activity in signaling contexts, and is inactivated by a point mutation to the conserved catalytic domain
IDA PMID:17156430 A role for Phospholipase D in Drosophila embryonic cellulari...
ACCEPT
Summary: Drosophila Pld has measured phospholipase D activity and a catalytic-site mutation abolishes the stimulated activity. This supports its defining lipid-hydrolysis activity independently of automated enzyme mappings.
Reason: Drosophila Pld has measured phospholipase D activity and a catalytic-site mutation abolishes the stimulated activity. This supports its defining lipid-hydrolysis activity independently of automated enzyme mappings.
D. melanogaster Pld exhibits classic Pld activity, increases its activity in signaling contexts, and is inactivated by a point mutation to the conserved catalytic domain
Summary: Drosophila Pld has measured phospholipase D activity and a catalytic-site mutation abolishes the stimulated activity. This supports its defining lipid-hydrolysis activity independently of automated enzyme mappings.
Reason: Drosophila Pld has measured phospholipase D activity and a catalytic-site mutation abolishes the stimulated activity. This supports its defining lipid-hydrolysis activity independently of automated enzyme mappings.
D. melanogaster Pld exhibits classic Pld activity, increases its activity in signaling contexts, and is inactivated by a point mutation to the conserved catalytic domain
Summary: Lipid metabolism is correct but broad: Pld hydrolyzes phosphatidylcholine and generates phosphatidic acid. The specific enzyme and product-biosynthesis terms capture its core function more clearly.
Reason: Lipid metabolism is correct but broad: Pld hydrolyzes phosphatidylcholine and generates phosphatidic acid. The specific enzyme and product-biosynthesis terms capture its core function more clearly.
D. melanogaster Pld exhibits classic Pld activity, increases its activity in signaling contexts, and is inactivated by a point mutation to the conserved catalytic domain
Summary: Hydrolysis of phosphatidylcholine by phospholipase D generates phosphatidic acid, the lipid product that mediates its membrane-trafficking and signaling functions.
Reason: Hydrolysis of phosphatidylcholine by phospholipase D generates phosphatidic acid, the lipid product that mediates its membrane-trafficking and signaling functions.
D. melanogaster Pld exhibits classic Pld activity, increases its activity in signaling contexts, and is inactivated by a point mutation to the conserved catalytic domain
IMP PMID:17156430 A role for Phospholipase D in Drosophila embryonic cellulari...
ACCEPT
Summary: Pld deficiency disrupts Golgi organization and secretory trafficking during cellularization, consistent with a core role in membrane trafficking through phosphatidic acid production.
Reason: Pld deficiency disrupts Golgi organization and secretory trafficking during cellularization, consistent with a core role in membrane trafficking through phosphatidic acid production.
IMP PMID:17156430 A role for Phospholipase D in Drosophila embryonic cellulari...
KEEP AS NON CORE
Summary: The loss-of-function phenotype demonstrates a contribution to embryonic cellularization through membrane trafficking. This developmental setting is a consequence of the core lipid-signaling mechanism.
Reason: The loss-of-function phenotype demonstrates a contribution to embryonic cellularization through membrane trafficking. This developmental setting is a consequence of the core lipid-signaling mechanism.
IMP PMID:15883198 Regulation of phototransduction responsiveness and retinal d...
KEEP AS NON CORE
Summary: Pld supports visual responsiveness and photoreceptor maintenance through phosphatidic-acid-dependent phosphoinositide homeostasis. The mutant phototransduction phenotype is supported, without implying that Pld itself is a photoreceptor.
Reason: Pld supports visual responsiveness and photoreceptor maintenance through phosphatidic-acid-dependent phosphoinositide homeostasis. The mutant phototransduction phenotype is supported, without implying that Pld itself is a photoreceptor.
Pld(null) flies exhibit decreased light sensitivity as well as a heightened susceptibility to retinal degeneration.
GO:0010004 gastrulation involving germ band extension
IMP PMID:17156430 A role for Phospholipase D in Drosophila embryonic cellulari...
KEEP AS NON CORE
Summary: Pld-null embryos show abnormal germ-band morphology and gastrulation, plausibly following the preceding cellularization defects. Retain the experimental developmental association as noncore rather than infer a separate direct gastrulation mechanism.
Reason: Pld-null embryos show abnormal germ-band morphology and gastrulation, plausibly following the preceding cellularization defects. Retain the experimental developmental association as noncore rather than infer a separate direct gastrulation mechanism.
Summary: Immunolocalization in cellularizing embryos places Pld in cytoplasmic vesicles, supporting an endomembrane-associated enzyme rather than an exclusively soluble or plasma-membrane-localized factor.
Reason: Immunolocalization in cellularizing embryos places Pld in cytoplasmic vesicles, supporting an endomembrane-associated enzyme rather than an exclusively soluble or plasma-membrane-localized factor.
In cellularizing embryos, Pld localized to the cytoplasm and/or to cytosolic vesicles of uniform small size evenly distributed between apical and basal regions of the blastoderm (Fig. 3A–D).
IDA PMID:17156430 A role for Phospholipase D in Drosophila embryonic cellulari...
ACCEPT
Summary: Immunolocalization in cellularizing embryos places Pld in cytoplasmic vesicles, supporting an endomembrane-associated enzyme rather than an exclusively soluble or plasma-membrane-localized factor.
Reason: Immunolocalization in cellularizing embryos places Pld in cytoplasmic vesicles, supporting an endomembrane-associated enzyme rather than an exclusively soluble or plasma-membrane-localized factor.
In cellularizing embryos, Pld localized to the cytoplasm and/or to cytosolic vesicles of uniform small size evenly distributed between apical and basal regions of the blastoderm (Fig. 3A–D).
Summary: The protein contains phosphoinositide-interaction architecture, but the accessible gene-specific data do not directly resolve binding of the parent phosphatidylinositol lipid versus its phosphorylated derivatives. The proposed interaction motif is supportive sequence context, not a measured ligand-specific binding assay.
Reason: The protein contains phosphoinositide-interaction architecture, but the accessible gene-specific data do not directly resolve binding of the parent phosphatidylinositol lipid versus its phosphorylated derivatives. The proposed interaction motif is supportive sequence context, not a measured ligand-specific binding assay.
Summary: Pld generates the signaling lipid phosphatidic acid and its activity is stimulated in signaling contexts. Its role in intracellular lipid signaling is supported by genetic and biochemical evidence.
Reason: Pld generates the signaling lipid phosphatidic acid and its activity is stimulated in signaling contexts. Its role in intracellular lipid signaling is supported by genetic and biochemical evidence.
D. melanogaster Pld exhibits classic Pld activity, increases its activity in signaling contexts, and is inactivated by a point mutation to the conserved catalytic domain
Pld(null) flies exhibit decreased light sensitivity as well as a heightened susceptibility to retinal degeneration.
GO:0048215 positive regulation of Golgi vesicle fusion to target membrane
IMP PMID:17156430 A role for Phospholipase D in Drosophila embryonic cellulari...
ACCEPT
Summary: Pld supports delivery and fusion competence of Golgi-derived vesicles during cellularization. The gene-specific study supports this regulatory process while leaving open the precise final membrane compartment.
Reason: Pld supports delivery and fusion competence of Golgi-derived vesicles during cellularization. The gene-specific study supports this regulatory process while leaving open the precise final membrane compartment.
D. melanogaster Pld exhibits classic Pld activity, increases its activity in signaling contexts, and is inactivated by a point mutation to the conserved catalytic domain
In cellularizing embryos, Pld localized to the cytoplasm and/or to cytosolic vesicles of uniform small size evenly distributed between apical and basal regions of the blastoderm (Fig. 3A–D).
These computational predictions are reviewed separately from the GOA annotation set used for this review. The assessments below are from this project and do not constitute official GO annotations or endorsement by GO/UniProt. They are not included in the existing annotation review above.
Lipid catabolism is supported but already implied by the characterized phospholipase reaction; cytoplasm is supported and less precise than cytoplasmic-vesicle localization.
Review rationale: Phosphatidylcholine hydrolysis is a lipid-catabolic reaction supported by measured Drosophila Pld activity. Although this exact biological-process ID is absent from the existing rows, the characterized D-type glycerophospholipase reaction already establishes the same lipid-breakdown biology, so it is correct but not biologically novel. This is reaction-level equivalence, not a claim that a molecular-function term is an ontology child of a biological-process term. The selected record retains both annotated PLD catalytic regions, supporting the broad reaction transfer.
Supporting Evidence:
PMID:15883198: "D. melanogaster Pld exhibits classic Pld activity, increases its activity in signaling contexts, and is inactivated by a point mutation to the conserved catalytic domain"
PMID:17156430: "Phospholipase D (PLD), which hydrolyzes the membrane phospholipid phosphatidylcholine to yield the lipid second messenger phosphatidic acid"
Review rationale: The cytoplasmic prediction is directly supported by immunolocalization in cellularizing embryos. It is broader than the existing cytoplasmic-vesicle localization, so it is less precise rather than an erroneous cytosolic default. The experiment describes both cytoplasm and cytosolic vesicles, without claiming exclusion from membrane-associated compartments.
Supporting Evidence:
PMID:17156430: "In cellularizing embryos, Pld localized to the cytoplasm and/or to cytosolic vesicles of uniform small size evenly distributed between apical and basal regions of the blastoderm (Fig. 3A–D)."