Essential Ca(2+)-independent role of the group IVA cytosolic phospholipase A(2) C2 domain for interfacial activity.

@article{Six2003EssentialCR,
  title={Essential Ca(2+)-independent role of the group IVA cytosolic phospholipase A(2) C2 domain for interfacial activity.},
  author={David A Six and Edward A. Dennis},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 26},
  pages={
          23842-50
        }
}
The cytosolic Group IVA phospholipase A2 (GIVAPLA2) translocates to intracellular membranes to catalyze the release of lysophospholipids and arachidonic acid. GIVAPLA2 translocation and subsequent activity is regulated by its Ca2+-dependent phospholipid binding C2 domain. Phosphatidylinositol 4,5-bisphosphate (PI-4,5-P2) also binds with high affinity and specificity to GIVAPLA2, facilitating membrane binding and activity. Herein, we demonstrate that GIVAPLA2 possessed full activity in the… CONTINUE READING
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Novel Role of GIVAPLA2 C2 Domain in Ca 2 -independent Activity

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