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Biochemical characterization of the L-plastin-actin interaction shows a resemblance with that of alpha-actinin and allows a distinction to be made between the two actin-binding domains of the molecule.

Abstract：

:Actin interaction with L-plastin, a plastin/fimbrins isoform of the alpha-actinin family of molecules, is poorly characterized, from the biochemical point of view. Besides, molecular modeling of the T-isoform has recently provided a complete model of interaction with filamentous actin [Volkmann, N., DeRosier, D., Matsudaira, P., and Hanein, D. (2001) J. Cell Biol. 153, 947-956]. In this study, we report that recombinant L-plastin binds actin in a manner that strongly resembles that of the alpha-actinin-actin interface. The similitudes concern the absence of specificity toward the actin isoform and the inhibition of the binding by phosphoinositides. Furthermore, the participation of actin peptides 112-125 and 360-372 in the interface together with an inhibition of the rate of pyrenyl F-actin depolymerization is in favor of a lateral binding of the plastin isoform along the filament axis and strenghtens the similitudes in the way L-plastin and alpha-actinin bind to actin. We have also investigated the functional aspect and the putative equivalence of the two actin-binding domains of L-plastin toward actin binding. We demonstrate for the first time that the two recombinant fragments, expressed as single domains, have different affinities for actin. We further analyzed the difference using chemical cross-linking and F-actin depolymerization experiments assayed by fluorescence and high-speed centrifugation. The results clearly demonstrate that the two actin-binding domains of plastin display different modes of interaction with the actin filament. We discuss these results in light of the model of actin interaction proposed for T-plastin.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Lebart MC,Hubert F,Boiteau C,Ventéo S,Roustan C,Benyamin Y

doi

10.1021/bi030151p

subject

Has Abstract

pub_date

2004-03-09 00:00:00

pages

2428-37

issue

eissn

0006-2960

issn

1520-4995

journal_volume

pub_type

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Biochemical characterization of the L-plastin-actin interaction shows a resemblance with that of alpha-actinin and allows a distinction to be made between the two actin-binding domains of the molecule.