In mammalian cells, there are three types of PLCs, *beta*, *gamma* and *delta*. Although the RhoGAP has been isolated and shown to activate PLC-*delta*1 by binding to it, most of the factors involved in the signal transduction pathway through PLC-*delta* are still unknown. In yeasts, only the *delta* type of PLC (Plc1p) has been detected. Some plc1 disruptants of S. cerevisiae are defective in growth under the high concentration of glucose, and a plc1 disruptant of S. pombe is sensitive to low pH and to NH4+. These defects indicate that Plc1p is important for sensing extracellular signals of nutrients and stress. Using immunochemical and two-hybrid protein interaction assays, we show that fission yeast Plc1p interacts with 14-3-3 proteins, Rad24p and Rad25p. A rad24 disruptant has been shown to be UV-sensitive. The plc1 disruptant also showed UV-sensitive phenotype, and the sensitivity of the plc1 rad24 double disruptant was not so different from those of single disruptants, an indication that Plc1p and Rad24p are involved in the same epistasis group with respect to UV sensitivity. Despite the previous report that 14-3-3 proteins are involved in DNA damage checkpoint, the duration of delay to mitosis after UV irradiation appeared to be normal in plc1 disruptants. Thus, Plc1p and 14-3-3 proteins were suggested to work together on the same pathway for response to UV irradiation, but not in DNA damage checkpoint pathway.