Phospho-cPLA2 translocates to membranes when intracellular calcium levels increase

Stable Identifier
R-HSA-111881
Type
Reaction [binding]
Species
Homo sapiens
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The 85kDa cytosolic phospholipase A2 (cPLA2 - PLA2G4A) is involved in cell signalling processes and inflammatory response and is regulated by phosphorylation and calcium concentrations. cPLA2 is phosphorylated at Ser727 and by a MAPK at Ser505. When phosphorylation is coupled with an influx of calcium ions, PLA2 becomes stimulated and translocates to the membrane where it releases arachidonic acid (AA) from membrane phospholipids. Calcium does not itself activate cPLA2. cPLA2 contains an N-terminal calcium-dependent phospholipid binding domain (CaLB) which shares homology with C2 domains (plays roles in signal transduction and membrane trafficking) and binds it to the membrane. Arachidonic acid is both a signalling molecule and the precursor for other signalling molecules termed eicosanoids (e.g., prostaglandins, leukotrienes and platelet-activating factor). A strict regulation of the activity of phospholipase enzyme is essential.

Literature References
PubMed ID Title Journal Year
9468497 Identification of the phosphorylation sites of cytosolic phospholipase A2 in agonist-stimulated human platelets and HeLa cells

Börsch-Haubold, AG, Bartoli, F, Asselin, J, Dudler, T, Kramer, RM, Apitz-Castro, R, Watson, SP, Gelb, MH

J Biol Chem 1998
1904318 A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP

Clark, JD, Lin, LL, Kriz, RW, Ramesha, CS, Sultzman, LA, Lin, AY, Milona, N, Knopf, JL

Cell 1991
11375391 Intracellular calcium signals regulating cytosolic phospholipase A2 translocation to internal membranes

Evans, JH, Spencer, DM, Zweifach, A, Leslie, CC

J Biol Chem 2001
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