PAI-1 Interacts with alfa Subunit of Proteasome and Modulates Its Activity

What is it about?

Plasminogen activator inhibitor type-1 (PAI-1), a multifunctional protein, is an important physiological regulator of fibrinolysis, extracellular matrix homeostasis and cell motility.Using the yeast two-hybrid system, we found that the α3 subunit of proteasome directly interacts with PAI-1.To ensure that the PAI-1-proteasome complex is formed in vivo, both proteins were coimmunoprecipitated from endothelial cells and identified with specific antibodies. Specificity of this interaction was evidenced after transfection of HeLa cells with pCMV-PAI-1 and coimmunoprecipitation of both proteins with anti-PAI-1 antibodies. of both proteins with anti-PAI-1 antibodies

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Why is it important?

Cellular distribution of PAI-1-proteasome complexes was established by immunogold staining and electron microscopy analyses.Both proteins appeared in a diffuse cytosolic pattern but also could be found in a dense perinuclear and nuclear location. Furthermore, PAI-1 induced formation of aggresomes freely located in endothelial cytoplasm.

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