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MBC in Press, published online ahead of print October 12, 2005
Mol. Biol. Cell 10.1091/mbc.E05-06-0545

A more recent version of this article appeared on January 1, 2006
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Submitted on June 17, 2005
Revised on September 18, 2005
Accepted on October 4, 2005

Phosphatidylinositol 4,5-Bisphosphate Anchors Cytosolic Group IVA Phospholipase A2 to Perinuclear Membranes and Decreases Its Calcium Requirement for Translocation in Live Cells

Javier Casas, Miguel A. Gijón, Ana G. Vigo, Mariano Sánchez Crespo, Jesús Balsinde, and María A. Balboa

Institute of Molecular Biology and Genetics, Spanish Research Council, 47003 Valladolid, Spain

Monitoring Editor: John York

The eicosanoids are centrally involved in the onset and resolution of inflammatory processes. A key enzyme in eicosanoid biosynthesis during inflammation is Group IVA phospholipase A2 (also known as cytosolic phospholipase A2{alpha}, cPLA2{alpha}). This enzyme is responsible for generating free arachidonate (AA) from membrane phospholipids. cPLA2{alpha} translocates to perinuclear membranes shortly after cell activation, in a process that is governed by the increased availability of intracellular Ca2+. However, cPLA2{alpha} also catalyzes membrane phospholipid hydrolysis in response to agonists that do not mobilize intracellular Ca2+. How cPLA2{alpha} interacts with membranes under these conditions is a major, still unresolved issue. Here we report that phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) promotes translocation of cPLA2{alpha} to perinuclear membranes of intact cells in a manner that is independent of rises in the intracellular Ca2+ concentration. PtdIns(4,5)P2 anchors the enzyme to perinuclear membranes and allows for a proper interaction with its phospholipid substrate to release arachidonate.

Address correspondence to: Jesús Balsinde (jbalsinde{at}ibgm.uva.es) or María A. Balboa (mbalboa{at}ibgm.uva.es)




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