Membrane-associated calcium-independent phospholipase A2c(iPLA2c) contains four potential in-frame methionine start sites (Mancuso, . Jenkins, . & Gross, . (2000)J. Biol. , 9937–9945), but the mechanisms regulating the types, amount and subcellular localization of iPLA2c in cells are incompletely understood. We now: (a) demonstrate the dramatic transcriptional repression of mRNAsynthesis encoding iPLA2cby a nucleotide sequence nested in the coding sequence itself; (b) localize the site of transcriptional repression to the most 5¢ sequence encoding the iPLA2choloprotein; (c) identify the presence of nuclear proteinconstituentswhichbind to the repressor regionbygel shift analysis;.
