The antenna model of actin-cable length control.


<p>(A) Smy1 proteins (red) are delivered to the formin (green) at the barbed end of the actin cable by myosin motors (yellow). Smy1 inhibits the polymerization activity of formins upon binding. The directed transport of Smy1 by myosin motors towards the formins leads to a length dependent average assembly rate <i>k</i><sub><i>on</i></sub>(<i>l</i>) = <i>wl</i>; the longer the cables, the larger the number of Smy1 proteins delivered, and consequently, smaller the average assembly rate. (B) A schematic showing all possible transitions between different chemical states in the antenna model. An uninhibited formin assembles cables at a constant rate <i>r</i>. Smy1+myosin complexes bind to formin at a rate <i>k</i><sub><i>on</i></sub>(<i>l</i>) = <i>wl</i> where, <i>l</i> is the length of the cable. Smy1 proteins detach from the formin with a rate <i>k</i><sub><i>off</i></sub>. Regardless of the state of the formin, i.e. whether it has Smy1 bound or not, the filament is disassembled by removal of subunits at a rate <i>d</i>.</p

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Last time updated on 12/02/2018

This paper was published in FigShare.

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