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Investigating the Molecular Basis of cPLA2α Membrane Bending
Author(s) -
Ward Katherine E,
Ropa James P,
Stahelin Robert V
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.587.3
Subject(s) - microbiology and biotechnology , endosome , cytosol , lipid bilayer , lipid raft , signal transduction , transfection , cytoplasm , biology , chemistry , membrane , biochemistry , gene , enzyme , intracellular
Signal transduction mediates disease through key molecular targets in the cell. As protein‐lipid interactions have been examined in the literature, their role in cellular signaling has become more prevalent. Lipid‐binding proteins have become high impact drug targets in cancer, inflammation and viral egress. One such target, termed cytosolic phospholipase A2 α (cPLA2α), has been shown to play a key role in the production of inflammatory mediators. A novel function of the protein was recently discovered in our lab showing that the cPLA2α C2 domain bends zwitterionic membranes, a process that is mediated by cPLA2α's ability to deeply penetrate the lipid bilayer. Others in the literature have reported cPLA2α to participate in Fc mediated phagocytosis, intra‐Golgi trafficking and endosomal trafficking further supporting cPLA2α's ability to bend membranes in cellular processes. In addition, direct evidence has been reported in the literature using siRNA showing that cPLA2α induced vesiculation in cells. These results translate into our cellular system as cells transfected with EGFP‐cPLA2α form cytoplasmic vesicular structures. We have preliminary evidence showing cPLA2α membrane bending is mediated by oligomerization. The origin of oligomerization is currently under further investigation using both in vitro and cellular techniques. This research is funded by AHA 11PRE7640028 and NIH T32GM075762