Probing phosphatidylinositolphosphates and adenosinenucleotides on talin nucleated actin polymerization
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Updated: Nov 3, 2026

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
Published on: March 28, 2008
G Isenberg1, V Niggli, U Pieper
1Technical University of Munich, Biophysics, Garching, Germany.
Abstract:
We have investigated the binding of PI, PIP and PIP2 to talin and the effect of phosphoinositides and adenosinenucleotides on talin-induced actin polymerization. At physiological salt concentrations, talin coprecipitates with liposomes when containing phosphoinositides but not when containing PI. The nucleating effect of talin as reflected by a twofold increase of fluorescence during the polymerization of actin labelled with NBD is not inhibited by phosphoinositides. The polymerization of ADP-actin versus ATP-actin was investigated in the presence and absence of talin by NBD fluorescence. ADP-actin nucleation induced by talin is comparably efficient as with ATP-actin. These experimental findings in summary have implications when evaluating the role of talin during cell activation.
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