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Probing phosphatidylinositolphosphates and adenosinenucleotides on talin nucleated actin polymerization
Author(s) -
Isenberg G.,
Niggli V.,
Pieper U.,
Kaufmann S.,
Goldmann W.H.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01203-3
Subject(s) - actin , polymerization , chemistry , biophysics , actina , pi , fluorescence , cytoskeleton , biochemistry , cell , biology , polymer , organic chemistry , physics , quantum mechanics
We have investigated the binding of PI, PIP and PIP 2 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.