Phosphorylation of p36 in vitro with pp60src. Regulation by Ca2+ and phospholipid.

P36 is a major substrate of the tyrosine protein kinases. P36 isolated from bovine intestine was used in phosphorylation reactions with pp60src. Phosphorylation was stimulated 3-5-fold by Ca2+, however the Km was the same (2.5 microM) at high or low Ca2+. Although the level of free Ca2+ needed for this enhanced phosphorylation was 10(-4)-10(-3) M, phosphatidylserine shifted the Ca2+ sensitivity to the 10(-6)-10(-5) M range. Independent evidence suggested that p36 interacts directly with liposomes containing phosphatidylserine. This raises the possibility that p36, like c-kinase, is a Ca2+-activated, phospholipid-dependent protein.