Phosphatidylinositol 3-kinase binds to profilin through the p85α subunit and regulates cytoskeletal assembly

Phosphatidylinositol 3-kinase (PI3-K), endowed with catalytic (110kDa) and regulatory (85kDa) subunits co-precipitates with anti-tyrosine antibodies in mitogen-activated cells. Association of PI3-K with cytoskeleton activates its catalytic activity through undeciphered mechanisms. Recently Singh et al., (Biochemistry, 35, 16544-16549, 1996) have shown that profilin activates PI3-K activity in a concentration-dependent manner. Consequently, we investigated the interaction between the PI3-K and profilin employing the GSTp85 alpha fusion protein and the results indicate a specific interaction between pofilin and p85 alpha. The effect of p85 alpha/profilin complex on polymerization of actin monomers was monitored fluorimetrically employing pyrene-labelled actin monomers. It was noted that p85 alpha/profilin complex on polymerization of actin monomers was monitored simultaneously bind to actin as well as to p85 alpha. The affinity of p85 alpha/profilin complex to actin increases in the presence of p85 alpha subunit of PI3-K as compared to profilin itself.