Actin-induced dimerization of palladin promotes actin-bundling.

ABSTRACT: A subset of actin binding proteins is able to form crosslinks between two or more actin filaments, thus producing structures of parallel or networked bundles. These actin crosslinking proteins interact with actin through either bivalent binding or dimerization. We recently identified two binding sites within the actin binding domain of palladin, an actin crosslinking protein that plays an important role in normal cell adhesion and motility during wound healing and embryonic development. In this study, we show that actin induces dimerization of palladin. Furthermore, the extent of dimerization reflects earlier comparisons of actin binding and bundling between different domains of palladin. On the basis of these results we hypothesized that actin binding may promote a conformational change t

SUBMITTER: Vattepu R 

PROVIDER: S-EPMC4282413 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature