We identified a putative Saccharomyces cerevisiae homolog of a phosphoinositide-specific phospholipase C (PI-PLC) gene, PLC), which encodes a protein most similar to the 8 class of PI-PLC enzymes. The PLC) gene was isolated during a study of PI-PLC-catalyzed hydrolysis of phospholipids to generate second-messenger molecules results from a wide range of stimuli and is implicated in many cellular processes, including mesoderm induction and axis determination in embryonic development (45), phototransduction (7,53,65,66,69,83), secretion (58), growth and differentiation (4, 13), muscle contraction (33), and long-term potentiation of synaptic transmission in memory (11). Recent evidence indicates that a PI signaling pathway exists for communication between the nucleus and the cytoplasm (14, 54). In addition, PIs are involved in regulating the organization of the cytoskeleton (21,22,55,67). Although many PI-PLC isozymes have been extensively characterized biochemically, the functions of the enzymes within any specific signal transduction pathway have not been elucidated, with the possible exception of the Drosophila PLC-P enzyme, which is known to be involved in phototransduction (7). Recently it was shown that mammalian PLC-11 is regulated by a G-protein-dependent mechanism (72,75,80) and that PLC--yl is regulated by tyrosine phosphorylation (35,47,49,79). It is likely that members of a particular PI-PLC subtype (e.g., 11, ,B2, and 13) are * Corresponding author. t Present address:
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