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Literature summary for 3.1.1.4 extracted from

  • Zizza, P.; Iurisci, C.; Bonazzi, M.; Cossart, P.; Leslie, C.C.; Corda, D.; Mariggio, S.
    Phospholipase A2IValpha regulates phagocytosis independent of its enzymatic activity (2012), J. Biol. Chem., 287, 16849-16859.
    View publication on PubMedView publication on EuropePMC
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Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
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 Mus musculus 5829
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Organism

Organism UniProt Comment Textmining
Mus musculus P47713
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-

Synonyms

Synonyms Comment Organism
phospholipase A2IValpha
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 Mus musculus
PLA2IValpha
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 Mus musculus

General Information

General Information Comment Organism
physiological function isoform PLA2IValpha is selectively activated upon Fc receptor-mediated phagocytosis in macrophages and rapidly translocates to the site of the nascent phagosome. Pharmacological inhibition of PLA2IValpha by pyrrophenone reduces particle internalization by up to 50%. Fibroblasts from PLA2IValpha knock-out mice overexpressing FcRIIA and able to internalize IgG-opsonized beads show 50% lower phagocytosis, compared with wild-type cells. Transfection of the catalytically inactive deleted PLA2IValpha mutant PLA2IValpha(1-525) and point mutant PLA2IValpha-S228C promotes recovery of this impaired function. Transfection of the PLA2IValpha C2 domain, but not of PLA2IValpha-D43N, which cannot bind to membranes, rescues FcR-mediated phagocytosis Mus musculus