Probing phosphatidylinositolphosphates and adenosinenucleotides on talin nucleated actin polymerization

FEBS Letters

Isenberg, G.¹  Niggli, V.²  Kaufmann, S.¹  Pieper, U.⁴  Goldmann, W.H.³ 

[1] Technical University of Munich, Biophysics E-22, James-Franck Str., D-85747 Garching, Germany;Department of Pathology, University of Bern, Murtenstr. 31, CH 3010 Bern, Switzerland;Surgery Research Laboratory, Massachusetts General Hospital, Harvard Medical School, Charlestown, MA 02129, USA;Institute of Physiological Chemistry, Ruhr University, D-44780 Bochum, Germany

关键词: Actin;    Talin;    Phosphoinositide;    ADP-actin polymerization;    PC;    phosphatidylcholine;    PS;    phosphatidylserine;    PIP2;    phosphatidyl-inositol-4;    5-diphosphate;    PIP;    phosphatidylinositol-4-monophosphate;    PI;    phosphatidylinositol;    NBD-actin;    7-chloro4-nitro-benzeno-2-oxa-1;    3-diazole actin;    ADP-actin;    adenosine 5′diphosphate;    ATP-actin;    adenosine 5′-triphosphate;   

DOI  :  10.1016/S0014-5793(96)01203-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown