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...

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Bibliographic Details
Published in:Biochemistry and molecular biology international Vol. 46; no. 2; pp. 241 - 248
Main Authors: Bhargavi, V., Chari, Veerendra B., Singh, Surya S.
Format: Journal Article
Language:English
Published: UK Informa Healthcare 01-10-1998
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Summary: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 GSTp85α fusion protein and the results indicate a specific interaction between pofilin and p85α. The effect of p85α/profilin complex on polymerization of actin monomers was monitored fluorimetrically employing pyrene‐labelled actin monomers. It was noted that p85α/profilin complex inhibits actin polymerization suggesting that profilin can simultaneously bind to actin as well as to p85α. The affinity of p85α/profilin complex to actin increases in the presence of p85α subunit of PI3‐K as compared to profilin itself.
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ISSN:1521-6543
1039-9712
1521-6551
DOI:10.1080/15216549800203752