Functional molecular imaging of ILK-mediated Akt/PKB signaling cascades and the associated role of beta-parvin.

Visualization and quantification of the dynamics of protein-protein interactions in living cells can be used to explore the macromolecular events involved in signal transduction processes. In this study, functional molecular imaging using a luciferase-based complementation method demonstrated how the integrin-linked kinase (ILK)-mediated protein complex controls downstream signals. The luciferase complementation ...
assay showed that Akt1 preferentially binds to beta-parvin rather than to ILK within the complex. Moreover, photon flux from the interaction between beta-parvin and Akt1 increased following serum stimulation, and the beta-parvin-Akt1 interaction was dependent on phosphoinositide 3-kinase. Intriguingly, small interfering (si)RNA-mediated beta-parvin knockdown increased photon flux from the interaction between ILK and Akt1, leading to stabilization of hypoxia-inducible factor-1alpha and increased expression of vascular endothelial growth factor-A. These data from functional molecular imaging demonstrated that beta-parvin plays a regulatory role in the ILK-mediated Akt (also called protein kinase B) signaling cascades, suggesting that beta-parvin might be a crucial modulator of cell survival.
Mesh Terms:
Actinin, Animals, Blotting, Western, Cell Line, Cell Survival, Humans, Hypoxia-Inducible Factor 1, Immunoprecipitation, Mice, NIH 3T3 Cells, Phosphatidylinositol 3-Kinases, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins c-akt, Reverse Transcriptase Polymerase Chain Reaction, Signal Transduction, Vascular Endothelial Growth Factor A
J. Cell. Sci.
Date: Mar. 01, 2010
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