title: The effect of alpha-actinin on the length distribution of F-actin.
abstract: Actin filament length distribution in cells is often regulated to fit specific tasks. In comparison to the well-studied regulation of the average filament length (e.g., using capping proteins), controlling the width of the distribution is less well understood. We utilize two complementary methods to measure the effect of alpha-actinin on the width of the distribution of lengths of F-actin in vitro. Analyzing transmission electron micrographs shows that crosslinking by alpha-actinin reduces the width of the length distribution of F-actin, decreasing the coefficient of variation by two- to threefold. Analysis of fluorescence data from depolymerization assays confirms this observation. We suggest a mechanistic molecular model in which a local (weak) stabilization of crosslinked monomers in the filament is the physical origin of the decrease in the variance of lengths. Although alpha-actinin is known to bind reversibly to F-actin, our model shows that even weak binding can produce this effect, and that in fact it persists throughout a wide range of binding strengths.
authors.affiliation: Department of Physics of Complex Systems, Weizmann Institute of Science, Rehovot, Israel. david.biron@weizmann.ac.il
authors.forename: D
authors.initials: D
authors.lastname: Biron
authors.forename: E
authors.initials: E
authors.lastname: Moses
mesh_terms: D008841:Actin Cytoskeleton / Q000737:chemistry; D000185:Actinin / Q000737:chemistry / Q000378:metabolism*; D000199:Actins / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D001703:Biophysics / Q000379:methods*; D003599:Cytoskeleton; D008840:Microfilament Proteins; D046529:Microscopy, Electron, Transmission / Q000379:methods*; D015233:Models, Statistical; D008962:Models, Theoretical; D018482:Muscle, Skeletal / Q000378:metabolism; D011485:Protein Binding; D011817:Rabbits; D013997:Time Factors
chemical_list: D000199:Actins; D008840:Microfilament Proteins; D000185:Actinin