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Phosphatidylinositol 3‐kinase binds to profilin through the p85α subunit and regulates cytoskeletal assembly
Author(s) -
Bhargavi V.,
Chari Veerendra B.,
Singh Surya S.
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800203752
Subject(s) - phosphatidylinositol , microbiology and biotechnology , profilin , cytoskeleton , protein subunit , chemistry , kinase , biology , biochemistry , actin cytoskeleton , gene , cell
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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