title: [Caldesmon changes the structure of actin at the leading edge and suppresses cell migration].
abstract: The effect of the suppression of expression of the actin-binding protein caldesmon on the motility of nonmuscle cells has been studied. A more than fivefold decrease in the content of this protein in cells by RNA interference led to the disturbance of the formation of actin stress fibrils and acceleration of cell migration to the zone of injury of the monolayer. A stimulation of stationary cells by serum induced a more than 1.5-fold accumulation of stress fibrils only in control cells but not in caldesmon-deficient cells. Similarly, the accumulation of actin filaments was observed in actively migrating cells of only wild type but not in cells with a low caldesmon content. These changes occurred mainly at the leading edge of the migrating cell where the distinct structure of actin filaments was not seen in the absence of caldesmon. It was assumed that caldesmon inhibits cell migration due to the stabilization of actin in filaments and a decrease in the dynamics of monomeric actin at the leading edge of the migrating cell.
authors.forename: T V
authors.initials: TV
authors.lastname: Kudriashova
authors.forename: P N
authors.initials: PN
authors.lastname: Rutkevich
authors.forename: A Ia
authors.initials: AIa
authors.lastname: Shevelev
authors.forename: T N
authors.initials: TN
authors.lastname: Vlasik
authors.forename: A V
authors.initials: AV
authors.lastname: Vorotnikov
mesh_terms: D008841:Actin Cytoskeleton / Q000648:ultrastructure; D000199:Actins / Q000648:ultrastructure*; D002148:Calmodulin-Binding Proteins / Q000096:biosynthesis / Q000502:physiology*; D002465:Cell Movement; D006367:HeLa Cells; D006801:Humans; D022502:Stress Fibers / Q000648:ultrastructure
chemical_list: D000199:Actins; D002148:Calmodulin-Binding Proteins