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Literature summary for 3.1.1.4 extracted from

  • Casas, J.; Meana, C.; Esquinas, E.; Valdearcos, M.; Pindado, J.; Balsinde, J.; Balboa, M.A.
    Requirement of JNK-mediated phosphorylation for translocation of group IVA phospholipase A2 to phagosomes in human macrophages (2009), J. Immunol., 183, 2767-2774.
    View publication on PubMed
Search for more literature for 3.1.1.4

Cloned(Commentary)

Cloned (Comment) Organism
macrophages transfected with the construct EGFP-cPLA2alpha, ECFP-S505A or ECFP-S505E Homo sapiens

Protein Variants

Protein Variants Comment Organism
S505A nonphosphorylatable mutant, does not translocate to the phagosomes Homo sapiens
S505E behavior is similar to that of the wild-type. Mutant that mimics phosphorylation on Ser505, translocates to the phagosomes. Makes the enzyme refractory to JNK inhibition, translocating normally to phagosomal membranes Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information inhibition of JNK activity inhibits the translocation of cPLA2alpha to phagosomal membranes Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
phagosome during phagocytosis, cPLA2alpha translocates to the phagosome. JNK regulates the translocation of cPLA2alpha to phagosomal membranes. Phosphorylation of cPLA2alpha is necessary for translocation Homo sapiens
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Source Tissue

Source Tissue Comment Organism Textmining

Synonyms

Synonyms Comment Organism
cPLA2alpha
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 Homo sapiens
cytosolic phospholipase A2alpha
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 Homo sapiens
group IVA phospholipase A2
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 Homo sapiens

General Information

General Information Comment Organism
physiological function a key role for JNK-mediated cPLA2alpha phosphorylation at Ser505 in the sequence of events leading to translocation and activation of the enzyme to phagosomal membranes in human macrophages Homo sapiens