The lack of interaction between vinculin and actin.
Vinculin was purified from chicken gizzard by a modification of the method of Feramisco and Burridge [1980; J Biol Chem 255:1194]. Vinculin did not alter the viscosity of actin as measured in an Ostwald viscometer, nor did it affect actin polymerization as measured with the fluorescent NBD-actin assay. Sedimentation experiments demonstrated that vinculin did not bind to actin, and electron microscopy of negatively stained specimens indicated that vinculin did not aggregate actin filaments into bundles. These results suggest that vinculin, by itself, does not interact with actin at least under commonly used conditions to assay actin-protein interactions in vitro.
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D008841:Actin Cytoskeleton / Q000502:physiology / Q000648:ultrastructure; D000199:Actins / Q000032:analysis / Q000502:physiology*; D000818:Animals; D002645:Chickens; D003432:Cross-Linking Reagents; D005895:Gizzard, Avian; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D009124:Muscle Proteins / Q000032:analysis / Q000502:physiology*; D014461:Ultracentrifugation; D016596:Vinculin; D014783:Viscosity
D000199:Actins; D003432:Cross-Linking Reagents; D046911:Macromolecular Substances; D009124:Muscle Proteins; D016596:Vinculin