Probing phosphatidylinositolphosphates and adenosinenucleotides on talin nucleated actin polymerization
- 18 November 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 397 (2-3) , 316-320
- https://doi.org/10.1016/s0014-5793(96)01203-3
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.Keywords
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