title: Length regulation of active biopolymers by molecular motors.
abstract: For biopolymers like cytoskeletal actin filaments and microtubules, assembly and disassembly are inherently dissipative processes. Molecular motors can affect the rates of subunit removal at filament ends. We introduce a driven lattice-gas model to study the effects of motor-induced depolymerization on the length of active biopolymers and find that increasing motor activity sharpens unimodal steady-state length distributions. Furthermore, for sufficiently fast moving motors, the relative width of the length distribution is determined only by the attachment rate of motors. Our results show how established molecular processes can be used to robustly regulate the size of cytoskeletal structures like mitotic spindles.
authors.affiliation: Theoretische Physik, Universität des Saarlandes, 66041 Saarbrücken, Germany.
authors.forename: Denis
authors.initials: D
authors.lastname: Johann
authors.forename: Christoph
authors.initials: C
authors.lastname: Erlenkämper
authors.forename: Karsten
authors.initials: K
authors.lastname: Kruse
mesh_terms: D000199:Actins / Q000737:chemistry / Q000378:metabolism; D001704:Biopolymers / Q000737:chemistry* / Q000378:metabolism*; D003198:Computer Simulation; D003598:Cytoskeletal Proteins / Q000737:chemistry / Q000378:metabolism; D003599:Cytoskeleton / Q000737:chemistry / Q000378:metabolism; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological; D008956:Models, Chemical; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000378:metabolism*; D013269:Stochastic Processes
chemical_list: D000199:Actins; D001704:Biopolymers; D003598:Cytoskeletal Proteins; D020409:Molecular Motor Proteins