The Saccharomyces cerevisiae SAC1 gene modulates yeast actin function and alleviates the essential requirement for phosphatidylinositol transfer protein (sec14p) activity in Golgi secretory function. The SAC1 gene product (Sac1p) is an integral membrane lipid phosphatase of the endoplasmic reticulum (ER) and the Golgi complex and contains a Sac phosphatase domain (1-2). Sac1p functions in a wide range of cellular processes including inositol metabolism, actin cytoskeletal organization, endoplasmic reticulum ATP transport, phosphatidylinositol-phospha-tidylcholine transfer protein function and multiple-drug sensitivity (3). Sac1p is an important regulator of microsomal ATP transport, providing a link between inositol phospholipid signaling and ATP-dependent processes in the yeast ER (4). Defects in Sac1p relieves the requirement for Sec14p by altering phospholipid metabolism to expand the pool of diacylglycerol in the Golgi (5). Sac1p dysfunction exerts its pleiotropic effects on yeast Golgi function, the organization of the actin cytoskeleton, and the cellular requirement for inositol, through altered metabolism of inositol glycerophospholipids (6). These effects suggest the secretory and cytoskeletal activities are coordinated to achieve proper spatial regulation of secretion in S. cerevisiae (7).